ID   PP62_ASFWA              Reviewed;         530 AA.
AC   P0CA08;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Polyprotein pp62 {ECO:0000250|UniProtKB:Q65179};
DE   AltName: Full=60 kDa polyprotein;
DE            Short=p60;
DE   AltName: Full=62 kDa polyprotein;
DE            Short=p62;
DE   Contains:
DE     RecName: Full=p15 {ECO:0000250|UniProtKB:Q65179};
DE     AltName: Full=PIG1;
DE   Contains:
DE     RecName: Full=p35 {ECO:0000250|UniProtKB:Q65179};
DE   Contains:
DE     RecName: Full=p8 {ECO:0000250|UniProtKB:Q65179};
GN   OrderedLocusNames=War-104;
OS   African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561444;
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: [Polyprotein pp62]: Essential for the correct assembly and
CC       maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}.
CC   -!- FUNCTION: [p35]: Component of the core shell (By similarity). Binds to
CC       phosphatidylserine, which may enable the core shell binding with the
CC       inner membrane (By similarity). {ECO:0000250|UniProtKB:Q65179}.
CC   -!- FUNCTION: [p15]: Component of the core shell (By similarity). Binds to
CC       phosphatidylserine and DNA, which may link the core shell to the inner
CC       membrane and to the viral nucleoid (By similarity).
CC       {ECO:0000250|UniProtKB:Q65179}.
CC   -!- FUNCTION: [p8]: Component of the core shell.
CC       {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SUBUNIT: [p35]: Monomer (By similarity). Predominantly exists as a
CC       monomer, with very little dimers (By similarity). Homodimerization
CC       seems to be linked to low pH (By similarity).
CC       {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SUBUNIT: [p15]: Homodimer; disulfide-linked (By similarity).
CC       Homotrimer; disulfide-linked (By similarity). Homohexamer (By
CC       similarity). {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SUBCELLULAR LOCATION: [Polyprotein pp62]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250|UniProtKB:Q65179}. Note=Found in
CC       perinuclear cytoplasmic viral factories during assembly.
CC       {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SUBCELLULAR LOCATION: [p35]: Virion {ECO:0000250|UniProtKB:Q65179}.
CC       Note=Located in the core shell, which functions like a matrix between
CC       the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SUBCELLULAR LOCATION: [p15]: Virion {ECO:0000250|UniProtKB:Q65179}.
CC       Note=Located in the core shell, which functions like a matrix between
CC       the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SUBCELLULAR LOCATION: [p8]: Virion {ECO:0000250|UniProtKB:Q65179}.
CC       Note=Located in the core shell, which functions like a matrix between
CC       the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000250|UniProtKB:Q65179}.
CC   -!- PTM: [p15]: Monoubiquitinated in vitro by viral UBCv1.
CC       {ECO:0000250|UniProtKB:P0CA06}.
CC   -!- PTM: [Polyprotein pp62]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. {ECO:0000250|UniProtKB:Q65179}.
CC   -!- SIMILARITY: Belongs to the asfivirus polyprotein pp62 family.
CC       {ECO:0000305}.
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DR   EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0CA08; -.
DR   PRIDE; P0CA08; -.
DR   Proteomes; UP000000858; Genome.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Disulfide bond; Host cytoplasm; Late protein; Ubl conjugation; Virion.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..530
FT                   /note="Polyprotein pp62"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000373461"
FT   CHAIN           2..158
FT                   /note="p15"
FT                   /id="PRO_0000373462"
FT   CHAIN           159..463
FT                   /note="p35"
FT                   /id="PRO_0000373463"
FT   CHAIN           464..530
FT                   /note="p8"
FT                   /id="PRO_0000373464"
FT   SITE            158..159
FT                   /note="Cleavage; by viral protease S273R"
FT                   /evidence="ECO:0000250|UniProtKB:Q65179"
FT   SITE            463..464
FT                   /note="Cleavage; by viral protease S273R"
FT                   /evidence="ECO:0000250|UniProtKB:Q65179"
SQ   SEQUENCE   530 AA;  60547 MW;  F35DDD14A041952A CRC64;
     MPSNMKQFCK ISVWLQQHDP DLLEIINNLC MLGNLSAAKY KHGVTFIYPK QAKIRDEIKK
     HAYSNDPSQA IKTLESLILP FYIPTPAEFT GEIGSYTGVK LEVEKTEANK VILKNGEAVL
     VPAADFKPFP DRRLAVWIME SGSMPLEGPP YKRKKEGGGN DPPVPKHISP YTPRTRIAIE
     VEKAFDDCMR QNWCSVNNPY LAKSVSLLSF LSLNHPTEFI KVLPLIDFDP LVTFYLLLEP
     YKTHGDDFLI PETILFGPTG WNGTDLYQSA MLEFKKFFTQ ITRQTFMDIA DSATKEVDVP
     ICYSDPETVH SYTNHVRTEI LHHNAVNKVT TPNLVVQAYN ELEQTNTIRH YGPIFPESTI
     NALRFWKKLW QDEQRFVIHG LHRTLMDQPT YETSEFAEIV RNLRFSRPGN NYINELNITS
     PAMYGDKHTT GDIAPNDRFA MLVAFINSTD FLYTAIPEEK VGGNETQTSS LTDLVPTRLH
     SFLNHNLSKL KILNRAQQTV RNILSNDCLN QLKHYVKHTG KNEILKLLQE