ID   PP220_ASFM2             Reviewed;        2475 AA.
AC   P0CA02;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 30.
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=Mal-100;
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.
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; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PRIDE; P0CA02; -.
DR   Proteomes; UP000000860; 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   CHAIN           2..44
FT                   /note="p5"
FT                   /id="PRO_0000454833"
FT   CHAIN           45..2475
FT                   /note="Polyprotein pp220"
FT                   /id="PRO_0000373428"
FT   CHAIN           45..368
FT                   /note="p34"
FT                   /id="PRO_0000373429"
FT   CHAIN           369..522
FT                   /note="p14"
FT                   /id="PRO_0000373430"
FT   CHAIN           523..893
FT                   /note="p37"
FT                   /id="PRO_0000373431"
FT   CHAIN           894..2475
FT                   /note="p150"
FT                   /id="PRO_0000373432"
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;  281036 MW;  F7440054C0FFCE5D CRC64;
     MGNRGSSTSS RPPLSSEANI YAKLQDHIQR QTRPFSGGGY FNGGGDKNPV QHIKDYHIDS
     VSSKAKLRII EGIIKAISKI GFKIDTKQPI EDILKDIKKQ LPDPRAGSTF VKNAEKQETV
     CKMIADAINQ EFIDLGQDKL IDTTEGAASI CRQIVLYINS LTHGLRAEYL DVHGSIENTL
     ENIKLLNDAI KQLHERMVTE VTKAAPNEEV INAVTMIEAV YRRLLNEQNL QISILTNFID
     NILTPTQKEL DKLQTDEVDI IKLLNDTNSV LGTKNFGKVL SYTLCNLGIA ASVANKINKA
     LQRVGLKVEQ YLQSKNWAEF DKELDLKRFS GLVSAENIAE FEKAVNLLRQ TFNERHKILE
     NNCAKKGGDE VKTPLDKRIE AQRLDRKHIL MEFLNKSTQA YNDFLENVKK IGIKLVKEIA
     LTPNITRLRD ALSRINDMGT IALDLSLIGF YTNAAAREER ETFLTQLTLV KNVLEEISKT
     DPNFKNLYDS CFRLLQIIDF YTDIVQKKYG GGEDCECTRV 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 KTLLEYLQHS ALSVGLKNLN QSEIGGQRMA LAQTAEEAAQ RVYLSTVRVN
     DALSSRWETE DMFFTFMLKS MAAKIFIVLG IYDMFERPEP VYKLIPTRMI LGGADELEPE
     VIPEAAELYF RLPRLAEFYQ KLFSFRDGNV QISMLPELEG IFSGLIRIIF MRPIELINIG
     DYSETEIRQL IKEINVIYQH FNLEYGEQEA TKKALIHFVN EINRRFGVIT RTEWEKFQRI
     VQEARTMNDF GMMNQTNYSI LPDEDGYTQS SQLLPSDRFI GPSSQPTPKW RPALYNIDSV
     DVQTGMLQPN SQWDLVQKFR KQLSEMFEDP SLQQELGKIS YQELIRQAIN ELKKEHTDKI
     QIVSKLIQGS ESLADTDVNK IFLFHETVIT GLNLLSAIYV LLNNFRNNIK GLDLDTIQKS
     IIEWLRETQP PDVNHANLLD WLGRKHGAIS EIRNPGLVVK ANNARLSEVY PDPTTDANTP
     QDRNLTTETL FAWIVQYVGI PAGGGVRPEQ ELAARYLVDN QRIMQLLLTN IFEITSSFNK
     MIQVRFPETS TAHVHLDFTG LISLIDSLMA DTKYFLDLLR PHIDKNIIQY YENRSNPGSF
     YWLEEHLIDK LIKPPTDARG RPLPGGELGL EGVNQIINKT YTLLTKPYNV LQLRGGAQRR
     DAANIQINNN PQSSERFEQY GRVFSKLVFY DALENNSGLR VEQVALGDFR LSNLIRTNNA
     QEENTLSYWD NIALRTYANV NDAANNLRRY RLYGSDYGIQ NNRSMMMVFN QLIASYITRF
     YDAPSGKIYL NLINAFANGN FSQAVMEMGY AHPDLARNNN AFGHRGDPTE QSVLLLSLGL
     ILQRLIKDTN RQGLSQHLIS TLTEIPIYLK ENYRANLPLF NKMFNILISQ GELLKQFIQY
     TNVQLARPNL TALLRANNDS VIYYNNNNVP MTGLSIGQAA MRGIGGVFRP NVTLMPLGDA
     QNNTSDIVRK RLVAVIDGII RGSHTLADSA MEVLHELTDH PIYLETEEHF IQNYMSRYNK
     EPLMPFSLSL YYLRDLRIEN NEVYDPLLYP NLESGSPEFK LLYGTRKLLG NDPVQLSDMP
     GVQLIMKNYN ETVVAREQIT PTRFEHFYTH AIQALRFIVN IRSFKTVMTY NENTFGGVNL
     ISEDRNDKPI ITAGIGMNAV YSLRKTLQDV ISFVESSYQE EQINNIHKIV SPKGQTRTLG
     SNRERERIFN LFDMNIIPIN VNALMRSIPL ANIYNYDYSF EEIACLMYGI SAEKVRSLNT
     AAPQPDVAEV LNIPNRPPIN TREFMLKLLI NPYVSVSITQ YGNELLSKGN AGYMSRIFRG
     DNALNMGRPK FLSDQIFNKV LFGSLYPTQF DYDEAGPSLA AGIQRGRERW GHPMSIYINQ
     ALHEIVRTIR LAETVRGLRN VIDRNQIIGE LNAFRTQLED TLREVNNLVQ TPEIQNNPTP
     EIIAAVQNWG QQYRAQITDL IDLIGNAGQA NSMISLIQNI NVQTAGAQLT ALFNRRGLPA
     PPPRQVLQND IEAIQWFMTI VINHPPILIA PFMLLVNNLK EFLNTLERYV YKTPRWLGPG
     TARIAQPPVG MAPGINMRHH TSYTENSVLT YITEQNREEG PWSIVKQVGV GIQKPTLVQI
     GKDRFDTRLI RNLIFITNVQ RLLRLRLNLE LSQFRNVLVS PDHIINPSIT EYGFSITGPS
     ETFSDKQYDS DIRIL