ID   PP220_ASFP4             Reviewed;        2475 AA.
AC   P0CA03;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Polyprotein pp220 {ECO:0000250|UniProtKB:Q08358};
DE   AltName: Full=220 kDa polyprotein;
DE   Contains:
DE     RecName: Full=p34 {ECO:0000250|UniProtKB:Q08358};
DE   Contains:
DE     RecName: Full=p14 {ECO:0000250|UniProtKB:Q08358};
DE   Contains:
DE     RecName: Full=p37 {ECO:0000250|UniProtKB:Q08358};
DE   Contains:
DE     RecName: Full=p150 {ECO:0000250|UniProtKB:Q08358};
DE   Contains:
DE     RecName: Full=p5 {ECO:0000250|UniProtKB:Q08358};
DE   Flags: Precursor;
GN   OrderedLocusNames=Pret-104;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
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 [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 pp220]: Essential for the core assembly. Its
CC       myristoyl moiety may function as a membrane-anchoring signal to bind
CC       the developing core shell to the inner viral envelope.
CC       {ECO:0000250|UniProtKB:Q08358}.
CC   -!- FUNCTION: [p34]: The structural protein p34 is a component of the virus
CC       core shell. {ECO:0000250|UniProtKB:Q08358}.
CC   -!- FUNCTION: [p14]: The structural protein p14 is a component of the virus
CC       core shell. {ECO:0000250|UniProtKB:Q08358}.
CC   -!- FUNCTION: [p37]: The structural protein p37 is a component of the virus
CC       core shell. {ECO:0000250|UniProtKB:Q08358}.
CC   -!- FUNCTION: [p150]: The structural protein p150 is a component of the
CC       virus core shell. {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SUBCELLULAR LOCATION: [Polyprotein pp220]: Host cytoplasm, host
CC       perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in
CC       perinuclear cytoplasmic viral factories during assembly.
CC       {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SUBCELLULAR LOCATION: [p34]: Virion {ECO:0000250|UniProtKB:Q08358}.
CC       Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}.
CC       Note=Found in perinuclear cytoplasmic viral factories during assembly
CC       (By similarity). In the virion, located in the core shell, which
CC       functions like a matrix between the DNA-containing nucleoid and the
CC       inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SUBCELLULAR LOCATION: [p14]: Virion {ECO:0000250|UniProtKB:Q08358}.
CC       Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}.
CC       Note=Found in perinuclear cytoplasmic viral factories during assembly.
CC       In the virion, located in the core shell, which functions like a matrix
CC       between the DNA-containing nucleoid and the inner envelope.
CC       {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SUBCELLULAR LOCATION: [p37]: Virion {ECO:0000250|UniProtKB:Q08358}.
CC       Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}.
CC       Host nucleus {ECO:0000250|UniProtKB:Q08358}. Note=Nuclear at early
CC       stages of infection. Found in perinuclear cytoplasmic viral factories
CC       during assembly. In the virion, located in the core shell, which
CC       functions like a matrix between the DNA-containing nucleoid and the
CC       inner envelope. {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SUBCELLULAR LOCATION: [p150]: Virion {ECO:0000250|UniProtKB:Q08358}.
CC       Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}.
CC       Note=Found in perinuclear cytoplasmic viral factories during assembly.
CC       In the virion, located in the core shell, which functions like a matrix
CC       between the DNA-containing nucleoid and the inner envelope.
CC       {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SUBCELLULAR LOCATION: [p5]: Virion {ECO:0000250|UniProtKB:Q08358}.
CC   -!- INDUCTION: [Polyprotein pp220]: Expressed in the late phase of the
CC       viral replicative cycle. {ECO:0000305}.
CC   -!- PTM: [Polyprotein pp220]: Specific enzymatic cleavages in vivo by the
CC       viral pS273R protease yield mature proteins.
CC       {ECO:0000250|UniProtKB:Q08358}.
CC   -!- SIMILARITY: Belongs to the asfivirus polyprotein pp220 family.
CC       {ECO:0000305}.
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DR   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PRIDE; P0CA03; -.
DR   Proteomes; UP000000859; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Coiled coil; Host cytoplasm; Host nucleus; Late protein; Lipoprotein;
KW   Myristate; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..44
FT                   /note="p5"
FT                   /id="PRO_0000454834"
FT   CHAIN           45..2475
FT                   /note="Polyprotein pp220"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000373434"
FT   CHAIN           45..368
FT                   /note="p34"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000373435"
FT   CHAIN           369..522
FT                   /note="p14"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000373436"
FT   CHAIN           523..893
FT                   /note="p37"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000373437"
FT   CHAIN           894..2475
FT                   /note="p150"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000373438"
FT   COILED          2184..2211
FT                   /evidence="ECO:0000255"
FT   SITE            44..45
FT                   /note="Cleavage; by viral protease S273R"
FT                   /evidence="ECO:0000250|UniProtKB:Q08358"
FT   SITE            368..369
FT                   /note="Cleavage; by viral protease S273R"
FT                   /evidence="ECO:0000250|UniProtKB:Q08358"
FT   SITE            522..523
FT                   /note="Cleavage; by viral protease S273R"
FT                   /evidence="ECO:0000250|UniProtKB:Q08358"
FT   SITE            893..894
FT                   /note="Cleavage; by viral protease S273R"
FT                   /evidence="ECO:0000250|UniProtKB:Q08358"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q08358"
SQ   SEQUENCE   2475 AA;  281269 MW;  E2F3F89B41C3F702 CRC64;
     MGNRGSSTSS RPPPSSEANI YAKLQDHIQR QTRPFSGGGY FNGGGDKNPV QHIKDYHIDS
     VSSKAKLRII EGIIRAIAKI GFKVDTKQPI EDILKDIKKQ LPDPRAGSTF VKNAEKQETV
     CKMIADAINQ EFIDLGQDKL IDTTEGAASI CRQIVLYINS LTHGLRAEYL DVHGSIENTL
     ENIKLLNDAI KQLHERMVTE VTKAAPNEEV INAVTMIEAV YRRLLNEQNL QINILTNFID
     NILTPTQKEL DKLQTDEVDI IKLLNDTNSV LGTKNFGKVL SYTLCNLGIA ASVANKINKA
     LQKVGLKVEQ YLQSKNWEEF DKELDLKRFS GLVSAENIAE FEKAVNLLRQ TFNERHKILE
     NSCAKKGGDE EKTPLDRRIE AQRLDRKHIL MEFLNKSTQA YNDFLENVKK IGIKLVKEIA
     LTPNITRLRD ALSRINDMGT IALDLSLIGF YTNAAAREER ETFLTQFMLV KNVLEEQSKT
     DPNFKNLYDS CSRLLQIIDF YTDIVQKKYG GEEDCECTRV GGAALTVEEL GLSKAARSQV
     DLNQAINTFM YYYYVAQIYS NLTHNKQEFQ SYEENYATIL GDAIAGRLMQ LDTEKNARIN
     SPAVDLARGH VGPNPGGAQE VDWKAAVSAI ELEYDVKRRF YRALEGLDLY LKNITKTFVN
     NIDSIQTVQQ MLDGVRIIGR WFTEATGDTL AQVFESFPTS AGNDSNVFTD NAPAGHYYEK
     VAAEIQQGRS VGTLRPVRAS QAKNIRDLIG RSLSNFQALK NIINAFARIG DMLGGEELRQ
     MVPMSPLQIY KTLLEYIQHS ALSVGLKNLN QSEIGGQRVA LARTPEEAAQ RVYLSTVRVN
     DALSTRWETE DVFFTFMLKS MAAKIFIVLG IYDMFERPEP VYKLIPTRMI LGGADELEPE
     VIPEAAELYF RLPRLAEFYQ KLFSFRDENV QISMLPELEG IFSGLIRIIF MRPIELINIG
     DYSETEIRQL IKEINVIYQH FNLEYGEQEA TKKALIHFVN EINRRFGVIT RTEWEKFQRI
     VQEARTMNDF GMMNQTNYSI LPDEDGYTQS SQLLPSDRFI SPSSQPTPKW RPALYNIDSV
     DVQTGMLQPN SQWDLVQKFR KQLSEMFEDP SLQQELGKVS YQELIRQAIN ELKKDHTDKI
     QIVSKLIQGS ESLADTDVNK IFLFHETVIT GLNLLSAIYV LLNNFRNNIK GLDLDTIQKS
     IIEWLRETPA NVNHANLIDW LGRKHGAISE IRNPGLVIKE INMRLSEVYP DPTTEANVPQ
     DRNLTTETLF AWIVPYVGIP AGGGVRAEQE LAARYLVDNQ RIMQLLLTNI FEMTSSFNKM
     VQVRFPETST AQVHLDFTGL ISLIDSLMAD TKYFLNLLRP HIDKNIIQYY ENRSNPGSFY
     WLEEHLIDKL IKPPTDAGGR PLPGGELGLE GVNQIINKTY TLLTKPYNVL QLRGGAQRRD
     AANIQINNNP QPSERFEQYG RVFSRLVFYD ALENNSGLRV EQVVLGDFRL SNLIRTNNAQ
     EENALSYWDN IALRTYANVN DAANNLRRYR LYGSDHGIQN NRSMMMVFNQ LVASYIARFY
     DAPSGKIYLN LINAFANGNF SQAVMEMGYA HPDLARNNNA FGHRGDPTEQ SVLLLSLGLI
     LQRLIKDTNR QGLSQHLIST LTEIPIYLKE NYRANLPLFN KMFNILISQG ELLKQFIQYT
     NVQLARPNLT ALLGANNDSV IYYNNNINVP MTGLSVGQAA MRGIGGVFRP NVTLMPLGDA
     QSNTSDIVRK RLVAVIDGII RGSHTLADSA MEVLHELTDH PIYLETEEHF IQNYMSRYNK
     EPLMPFSLSL YYLRDLRIEN NEVYDPLLYP NLESGSPEFK LLYGTRKLLG NDPVQLSDMP
     GVQLIMKNYN ETVVAREQIT PTRFEHFYTH AIQALRFIIN IRSFKTVMMY NENTFGGVNL
     ISENRDDKPI ITAGIGMNAV YSLRKTLQDV ISFVESSYQE EQINHIHKIV SPKGQTRTLG
     SNRERERIFN LFDMNIIPIN VNALMRSIPL ANIYNYDYSF EEIACLMYGI SAEKVRSLNT
     AAPQPDIAEV LNIPNRPPMN TREFMLKLLI NPYVSVSITQ YGNELLSKGN AGYMSRIFRG
     DNALNMGRPK FLSDQIFNKV LFGSLYPTQF DYDEAGPSLA AGIQRGRERW GHPMSIYINQ
     ALHEIVRTIR LAETVRGLRN VIDRNQIIGE LNAFRTQLED TRREVNNLIQ TPEIRNNPTP
     EIIAAVQNWG QQYRGQITDL IDLIGNVGQA NSMINLIQNI TPQTAGAQLI ALFNIRGLPA
     PPPRQVIQND IEAMQWFMTM VINHPPILIA PFMLLVNNLK EFLNTLERYV YKTPRWLGPG
     TARIAQPPVG MAPGINMRHH TSYTENSVLT YITEQNREEG PWSIVKQVGV GIQKPTLVQI
     GKDRFDTRLI RNLIFITNIQ RLLRLRLNLE LSQFRNVLVS PDHIINPSIT EYGFSITGPS
     ETFSDKQYDS DIRIL