PP62_ASFB7
ID PP62_ASFB7 Reviewed; 530 AA.
AC Q65179; Q86851;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Polyprotein pp62 {ECO:0000303|PubMed:30185597};
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:0000303|PubMed:30185597};
DE Contains:
DE RecName: Full=p35 {ECO:0000303|PubMed:30185597};
DE AltName: Full=PIG1;
DE AltName: Full=UB18;
DE Contains:
DE RecName: Full=p8 {ECO:0000303|PubMed:30185597};
GN OrderedLocusNames=Ba71V-94; ORFNames=CP530R;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-277, PROTEIN SEQUENCE OF 2-8, AND
RP UBIQUITINATION (P15).
RC STRAIN=BA71V, and Isolate Uganda;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=8474154; DOI=10.1128/jvi.67.5.2475-2485.1993;
RA Prados F.J., Vinuela E., Alcami A.;
RT "Sequence and characterization of the major early phosphoprotein p32 of
RT African swine fever virus.";
RL J. Virol. 67:2475-2485(1993).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN (POLYPROTEIN PP62), AND SUBCELLULAR
RP LOCATION (POLYPROTEIN PP62).
RX PubMed=9223468; DOI=10.1128/jvi.71.8.5799-5804.1997;
RA Simon-Mateo C., Andres G., Almazan F., Vinuela E.;
RT "Proteolytic processing in African swine fever virus: evidence for a new
RT structural polyprotein, pp62.";
RL J. Virol. 71:5799-5804(1997).
RN [5]
RP SUBCELLULAR LOCATION (P35), AND SUBCELLULAR LOCATION (P15).
RX PubMed=33629764; DOI=10.1096/fj.202002145r;
RA Andres G., Alejo A., Salas J., Salas M.L.;
RT "African swine fever virus polyproteins pp220 and pp62 assemble into the
RT core shell.";
RL J. Virol. 76:12473-12482(2002).
RN [6]
RP FUNCTION.
RX PubMed=19846532; DOI=10.1128/jvi.01858-09;
RA Suarez C., Salas M.L., Rodriguez J.M.;
RT "African swine fever virus polyprotein pp62 is essential for viral core
RT development.";
RL J. Virol. 84:176-187(2010).
RN [7]
RP SUBCELLULAR LOCATION (P35), SUBCELLULAR LOCATION (P15), SUBCELLULAR
RP LOCATION (P8), PROTEOLYTIC CLEAVAGE (POLYPROTEIN PP62), FUNCTION (P35),
RP FUNCTION (P15), AND FUNCTION (P8).
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 [8]
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).
RN [9] {ECO:0007744|PDB:7BQA}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 161-464, SUBUNIT (P35), AND
RP FUNCTION (P35).
RX PubMed=32519301; DOI=10.1007/s13238-020-00730-w;
RA Li G., Fu D., Zhang G., Zhao D., Li M., Geng X., Sun D., Wang Y., Chen C.,
RA Jiao P., Cao L., Guo Y., Rao Z.;
RT "Crystal structure of the African swine fever virus structural protein p35
RT reveals its role for core shell assembly.";
RL Protein Cell 11:600-605(2020).
RN [10] {ECO:0007744|PDB:7BQ9}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 2-160, SUBUNIT (P15), AND
RP FUNCTION (P15).
RX PubMed=32451720; DOI=10.1007/s13238-020-00731-9;
RA Fu D., Zhao D., Zhang W., Zhang G., Li M., Zhang Z., Wang Y., Sun D.,
RA Jiao P., Chen C., Guo Y., Rao Z.;
RT "Structure of African swine fever virus p15 reveals its dual role for
RT membrane-association and DNA binding.";
RL Protein Cell 11:606-612(2020).
RN [11] {ECO:0007744|PDB:7CP2}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 2-153.
RA Liu K.F., Meng Y.M., Chai Y., Li L.J., Sun H., Gao G.F., Tan S.G., Qi J.X.;
RT "Crystal structure of the African swine fever virus core shell protein
RT p15.";
RL Submitted (AUG-2020) to the PDB data bank.
CC -!- FUNCTION: [Polyprotein pp62]: Essential for the correct assembly and
CC maturation of the core of the virion. {ECO:0000269|PubMed:19846532}.
CC -!- FUNCTION: [p35]: Component of the core shell (PubMed:30185597). Binds
CC to phosphatidylserine, which may enable the core shell binding with the
CC inner membrane (PubMed:32519301). {ECO:0000269|PubMed:30185597,
CC ECO:0000269|PubMed:32519301}.
CC -!- FUNCTION: [p15]: Component of the core shell (PubMed:30185597). Binds
CC to phosphatidylserine and DNA, which may link the core shell to the
CC inner membrane and to the viral nucleoid (PubMed:32451720).
CC {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:32451720}.
CC -!- FUNCTION: [p8]: Component of the core shell.
CC {ECO:0000269|PubMed:30185597}.
CC -!- SUBUNIT: [p35]: Monomer (PubMed:32519301). Predominantly exists as a
CC monomer, with very little dimers (PubMed:32519301). Homodimerization
CC seems to be linked to low pH (PubMed:32519301).
CC {ECO:0000269|PubMed:32519301}.
CC -!- SUBUNIT: [p15]: Homodimer; disulfide-linked (PubMed:32451720,
CC PubMed:33629764). Homotrimer; disulfide-linked (PubMed:33629764).
CC Homohexamer (PubMed:32451720). {ECO:0000269|PubMed:32451720,
CC ECO:0000269|PubMed:33629764}.
CC -!- SUBCELLULAR LOCATION: [Polyprotein pp62]: Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:9223468}. Note=Found in
CC perinuclear cytoplasmic viral factories during assembly.
CC {ECO:0000269|PubMed:9223468}.
CC -!- SUBCELLULAR LOCATION: [p35]: Virion {ECO:0000269|PubMed:30185597,
CC ECO:0000269|PubMed:33629764}. Note=Located in the core shell, which
CC functions like a matrix between the DNA and the inner envelope.
CC {ECO:0000269|PubMed:33629764}.
CC -!- SUBCELLULAR LOCATION: [p15]: Virion {ECO:0000269|PubMed:30185597,
CC ECO:0000269|PubMed:33629764}. Note=Located in the core shell, which
CC functions like a matrix between the DNA and the inner envelope.
CC {ECO:0000269|PubMed:33629764}.
CC -!- SUBCELLULAR LOCATION: [p8]: Virion {ECO:0000269|PubMed:30185597}.
CC Note=Located in the core shell, which functions like a matrix between
CC the DNA and the inner envelope. {ECO:0000303|PubMed:30185597}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923}.
CC -!- PTM: [p15]: Monoubiquitinated in vitro by viral UBCv1.
CC {ECO:0000269|PubMed:7853518}.
CC -!- PTM: [Polyprotein pp62]: Specific enzymatic cleavages in vivo by the
CC viral pS273R protease yield mature proteins.
CC {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:9223468}.
CC -!- SIMILARITY: Belongs to the asfivirus polyprotein pp62 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB33353.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18466; AAA65323.1; -; Genomic_DNA.
DR EMBL; S75219; AAB33353.1; ALT_FRAME; mRNA.
DR EMBL; M96354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_042787.1; NC_001659.2.
DR PDB; 6LNL; X-ray; 1.93 A; A/B/C=1-160.
DR PDB; 6NLN; X-ray; 1.93 A; A/B/C=2-160.
DR PDB; 7BQ9; X-ray; 2.61 A; A/B=2-160.
DR PDB; 7BQA; X-ray; 2.10 A; A/B=161-464.
DR PDB; 7CP2; X-ray; 2.19 A; A/B/C=2-153.
DR PDBsum; 6LNL; -.
DR PDBsum; 6NLN; -.
DR PDBsum; 7BQ9; -.
DR PDBsum; 7BQA; -.
DR PDBsum; 7CP2; -.
DR SMR; Q65179; -.
DR GeneID; 22220323; -.
DR KEGG; vg:22220323; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019069; P:viral capsid assembly; IDA:CACAO.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Host cytoplasm;
KW Late protein; Reference proteome; Ubl conjugation; Virion.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7853518"
FT CHAIN 2..530
FT /note="Polyprotein pp62"
FT /id="PRO_0000373445"
FT CHAIN 2..158
FT /note="p15"
FT /id="PRO_0000373446"
FT CHAIN 159..463
FT /note="p35"
FT /id="PRO_0000373447"
FT CHAIN 464..530
FT /note="p8"
FT /id="PRO_0000373448"
FT SITE 10
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:33629764"
FT SITE 39
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:33629764"
FT SITE 158..159
FT /note="Cleavage; by viral protease S273R"
FT /evidence="ECO:0000305|PubMed:30185597"
FT SITE 463..464
FT /note="Cleavage; by viral protease S273R"
FT /evidence="ECO:0000305|PubMed:30185597"
FT DISULFID 9
FT /note="Interchain (with C-30)"
FT /evidence="ECO:0000269|PubMed:33629764"
FT DISULFID 30
FT /note="Interchain (with C-9)"
FT /evidence="ECO:0000269|PubMed:33629764"
FT VARIANT 16
FT /note="Q -> H (in strain: Isolate Uganda)"
FT VARIANT 87
FT /note="A -> M (in strain: Isolate Uganda)"
FT VARIANT 106
FT /note="T -> K (in strain: Isolate Uganda)"
FT VARIANT 121
FT /note="V -> I (in strain: Isolate Uganda)"
FT VARIANT 131
FT /note="D -> N (in strain: Isolate Uganda)"
FT VARIANT 135
FT /note="A -> T (in strain: Isolate Uganda)"
FT VARIANT 141
FT /note="S -> A (in strain: Isolate Uganda)"
FT VARIANT 165
FT /note="P -> S (in strain: Isolate Uganda)"
FT MUTAGEN 10
FT /note="K->A: Complete loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:33629764"
FT MUTAGEN 39
FT /note="K->A: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:33629764"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6LNL"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:6LNL"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:6LNL"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:6LNL"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7BQ9"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:6LNL"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:6LNL"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:6LNL"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6LNL"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6LNL"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6LNL"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6LNL"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6LNL"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6LNL"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:6LNL"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:7BQA"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:7BQA"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:7BQA"
FT TURN 362..366
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 367..387
FT /evidence="ECO:0007829|PDB:7BQA"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 393..405
FT /evidence="ECO:0007829|PDB:7BQA"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:7BQA"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:7BQA"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:7BQA"
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
