PP62_ASFM2
ID PP62_ASFM2 Reviewed; 530 AA.
AC P0CA06;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Polyprotein pp62;
DE AltName: Full=60 kDa polyprotein {ECO:0000250|UniProtKB:Q65179};
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=Mal-102;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
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]
RP SUBCELLULAR LOCATION (P15), AND UBIQUITINATION (P15).
RX PubMed=7853518; DOI=10.1128/jvi.69.3.1785-1793.1995;
RA Hingamp P.M., Leyland M.L., Webb J., Twigger S., Mayer R.J., Dixon L.K.;
RT "Characterization of a ubiquitinated protein which is externally located in
RT African swine fever virions.";
RL J. Virol. 69:1785-1793(1995).
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:0000269|PubMed:7853518}.
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:0000269|PubMed:7853518}.
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; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0CA06; -.
DR Proteomes; UP000000860; Genome.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Disulfide bond; Host cytoplasm; Late protein; Ubl conjugation; Virion.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q65179"
FT CHAIN 2..530
FT /note="Polyprotein pp62"
FT /id="PRO_0000373453"
FT CHAIN 2..158
FT /note="p15"
FT /id="PRO_0000373454"
FT CHAIN 159..463
FT /note="p35"
FT /id="PRO_0000373455"
FT CHAIN 464..530
FT /note="p8"
FT /id="PRO_0000373456"
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; 60563 MW; 456A2C7EC9B61B88 CRC64;
MPSNMKQFCK ISVWLQQHDP DLLEIINNLC MLGNLSAAKY KHGVTFIYPK QAKIRDEIKK
HAYSNDPSQA IKTLESLILP FYIPTPAEFT GEIGSYTGVK LEVEKTEANK VILKNGEAVL
IPAADFKPFP DRRLAVWIME SGSMPLEGPP YKRKKEGGGN DPPVPKHISP YTPRTRIAIE
VEKAFDDCMR QNWCSVNNPY LAKSVSLLSF LSLNHPTEFI KVLPLIDFDP LVTFYLLLEP
YKTHGDDFLI PETVLFGPTG WNGTDLYQSA MLEFKKFFTQ ITRQTFMDIA DTATKEVDVP
ICYSDPETVH SYANHVRTEI LHHNMVNKVT TPNLVVQAYN ELEQTNTIRH YGPIFPESTI
NALRFWKKLW QDEQRFVIHG LHRTLMDQPT YETSEFAEIV RNLRFSRPGN NYINELNITS
PAMYGDKHTT GDIAPNDRFA MLVAFINSTD FLYTAIPEEK VGGNDTQTSS LTDLVPTRLH
SFLNHNLSKL KILNRAQQTV RNILSNDCLN QLKHYVKHTG KNEILKLLQD
