PP62_ASFK5
ID PP62_ASFK5 Reviewed; 534 AA.
AC P0CA05;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 23-FEB-2022, entry version 21.
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=Ken-106;
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.
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 -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- PTM: [p15]: Monoubiquitinated in vitro by viral UBCv1.
CC {ECO:0000250|UniProtKB:Q65179}.
CC -!- PTM: [Polyprotein pp62]: Specific enzymatic cleavages in vivo by the
CC viral pS273R protease yield mature proteins.
CC {ECO:0000250|UniProtKB:Q65179}.
CC -!- SIMILARITY: Belongs to the asfivirus polyprotein pp62 family.
CC {ECO:0000305}.
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DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0CA05; -.
DR Proteomes; UP000000861; 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; Ubl conjugation; Virion.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q65179"
FT CHAIN 2..534
FT /note="Polyprotein pp62"
FT /id="PRO_0000373449"
FT CHAIN 2..158
FT /note="p15"
FT /id="PRO_0000373450"
FT CHAIN 159..463
FT /note="p35"
FT /id="PRO_0000373451"
FT CHAIN 464..534
FT /note="p8"
FT /id="PRO_0000373452"
FT SITE 10
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q65179"
FT SITE 39
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q65179"
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"
FT DISULFID 9
FT /note="Interchain (with C-30)"
FT /evidence="ECO:0000250|UniProtKB:Q65179"
FT DISULFID 30
FT /note="Interchain (with C-9)"
FT /evidence="ECO:0000250|UniProtKB:Q65179"
SQ SEQUENCE 534 AA; 61028 MW; 7B6AF7D6C6C71FBE CRC64;
MPSNMKQFCK ISVWLQQHDP DLLEIINNLC MLGNLSAAKY KHGVTFIYPK QAKIRDEIKK
HAYSNDPSQA IKTLESLILP FYIPTPMEFT GEIGSYTGVK LEVEKKEANK VILKNGEAVL
IPAADFKPFP DRRLAVWIME SGSMPLEGPP YKRKKEGGGN DPPVSKHISP YTPRTRIAIE
VEKAFDECMR QNWCSVNNPY LAKSVSLLSF LSLNHPTEFI KVLPLIDFDP LVTFYLLLEP
YKTHGDDFLI PETILFGPTG WNGTDLYQSA MLEFKKFFTQ ITRQTFMDIA DTATKEVDVP
ICYSDPETVH SYANHVRTEI LHHNMVNKVT TPNLVVQAYN ELEQTNTIRH YGPIFPESTI
NALRFWKKLW QDEQRFVIHG LHRTLMDQPT YETSEFAEIV RNLRFSRPGN NYINELNITS
PAMYGDKHTT GDIAPNDRFA MLVAFINSTD FLYTAIPEEK VGGNDTQTGS QTSSLTDLVP
TRLHSFLNHN LSKLKILNRA QQTVKNILSN DCLNQLKHYV KHTGKNEILK LLQE
