VPRT_ASFK5
ID VPRT_ASFK5 Reviewed; 273 AA.
AC P0C9B9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=SUMO-1 cysteine protease S273R {ECO:0000303|PubMed:32075933};
DE Short=pS273R;
DE EC=3.4.22.-;
GN OrderedLocusNames=Ken-123;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
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.
RN [2] {ECO:0007744|PDB:6LJ9, ECO:0007744|PDB:6LJB}
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=32075933; DOI=10.1128/jvi.02125-19;
RA Li G., Liu X., Yang M., Zhang G., Wang Z., Guo K., Gao Y., Jiao P., Sun J.,
RA Chen C., Wang H., Deng W., Xiao H., Li S., Wu H., Wang Y., Cao L., Jia Z.,
RA Shang L., Yang C., Guo Y., Rao Z.;
RT "Crystal Structure of African Swine Fever Virus pS273R Protease and
RT Implications for Inhibitor Design.";
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:32075933}.
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 in the late phase of the viral replicative cycle.
CC {ECO:0000250|UniProtKB:Q00946}.
CC -!- SIMILARITY: Belongs to the peptidase C63 family. {ECO:0000305}.
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DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6LJ9; X-ray; 2.31 A; A/B=1-273.
DR PDB; 6LJB; X-ray; 2.49 A; A=1-273.
DR PDBsum; 6LJ9; -.
DR PDBsum; 6LJB; -.
DR SMR; P0C9B9; -.
DR Proteomes; UP000000861; 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 3D-structure; Host cytoplasm; Hydrolase; Late protein; Protease;
KW Thiol protease; Virion.
FT CHAIN 1..273
FT /note="SUMO-1 cysteine protease S273R"
FT /id="PRO_0000373129"
FT ACT_SITE 168
FT /evidence="ECO:0000305|PubMed:32075933"
FT ACT_SITE 187
FT /evidence="ECO:0000305|PubMed:32075933"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:32075933"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:6LJ9"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6LJ9"
FT TURN 115..119
FT /evidence="ECO:0007829|PDB:6LJB"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:6LJB"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:6LJ9"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:6LJ9"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:6LJ9"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:6LJ9"
SQ SEQUENCE 273 AA; 31609 MW; EC9F1C86A4DDA824 CRC64;
MSILEKITSS PSECAEHITN KDSCLSKKIQ KELTSFLQKK ETLGCDSESC VITHPAVKAY
AQQKGLDLSK ELETRFKAPG PRNNTGLLTN FNIDETLQRW AIKYTKFFNC PFSMMDFERI
HYKFNQVDMV KVYKGEELQY VEGKAVKRPC NTFGCVLNTD FSTGTGKHWV AIFVDMRGDC
WSIEYFNSAG NSPPGPVIRW MERVKQQLLK IHHTVKTLAV TNIRHQRSQT ECGPYSLFYI
RARLDNVSYT HFISTRITDE EMYKFRTHLF RIA
