ID   PP220_ASFK5             Reviewed;        2475 AA.
AC   P0CA01;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   23-FEB-2022, entry version 25.
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=Ken-104;
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 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=Localizes to the viral factory at 16 hpi. In the virion, located
CC       in the core shell, which functions like a matrix between the DNA-
CC       containing nucleoid and the inner envelope.
CC       {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=Found in perinuclear
CC       cytoplasmic viral factories during assembly. In the virion, located in
CC       the core shell, which functions like a matrix between the DNA-
CC       containing nucleoid and the inner envelope.
CC       {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: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- PTM: [Polyprotein pp220]: The polyprotein is not glycosylated.
CC       {ECO:0000250|UniProtKB:Q08358}.
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000861; 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"
FT   CHAIN           2..44
FT                   /note="p5"
FT                   /id="PRO_0000454832"
FT   CHAIN           45..2475
FT                   /note="Polyprotein pp220"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000373422"
FT   CHAIN           45..368
FT                   /note="p34"
FT                   /id="PRO_0000373423"
FT   CHAIN           369..522
FT                   /note="p14"
FT                   /id="PRO_0000373424"
FT   CHAIN           523..893
FT                   /note="p37"
FT                   /id="PRO_0000373425"
FT   CHAIN           894..2475
FT                   /note="p150"
FT                   /id="PRO_0000373426"
FT   COILED          2185..2212
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;  281392 MW;  4FAE3DBF0784C7D5 CRC64;
     MGNRGSSTSS RPPLSSEANL YAKLQDHIQR QTRPFSGGGY FNGGGDKNPV QHIKDYHIDS
     VSSKAKLRII EGIIKAISKI GFKVDTKQPI EDILKDIKKQ LPDPRAGSTF VKNAEKQETI
     CKMIADAINQ EFIDLGQDKL IDTTEGAASI CRQIVLYINS LTHGLRAEYL DVHGSIENTL
     ENIKLLSDAI KQLHERMVTE VTKAAPNEEV INAVTMIEAV YRRLLNEQNL QINILTNFID
     NILTPTQKEL DKLKTDEVDI IKILNDTNSV LGTKNFGKVL SYTLCNLGIA ATVANKINKA
     LQRVGLKVEQ YLHSKNWAEF DKELDLKRFS GLVSAENIAE FEKAVNLLRQ TFNERHKILE
     NNCAKKGGDG EKTPLDKRME AQRLDRKHIL MEFLNKSTQA YNDFLENVKK IGMKLVKEIA
     LTPNITKLRD ALSRINDMGT IALDLSLIGF YNNAAAREER ETFLIQLTLV KNVLEELAKT
     DPNFKNLYDS CFRLLQIIDF YTDIVQKKYG GGEDCECTKV GGAALTVEEL GLSKAARSQV
     DLNQAINTFM YYYYVAQIYS NLTHNKQEFQ SYEENYATIL GDAIAGRLMQ LDTEKNARIN
     SPAVDLARGH VGPNPGGAQE VDWKATISAI ELEYDVKRRF YRALEGLDLY LKNITKTFVN
     NIDSIQTVQQ MLDGVRIIGR WFTEATGDTL AQVFESFPTS AGNDSNVFTD NAPAGHYYEK
     VAAEIQQGRG VGTLRPVRAS QAKNIRDLIG RSLSNFQALK NIINAFARIG DMLGGEELRQ
     TVPMSPLQIY KTLLEYIQHS ALSVGLKNLN QTQIGGQRVA LAQTAEEASQ RVYLSTVRVN
     DALSTRWETE DVFFTFMLKS MAAKIFIVLG IYDMFERPEP VYKLIPTRMI LGGADELEPE
     VIPEAAGLYF RLPRLAEFYQ KLFSFRDENV QISMLPELEG IFSGLIRVIF MRPIELINIG
     DYSETEIRQL IKEINVIYQH FNLEYGEQEA VKKALIHFVN EINRRFGVIT RTEWEKFQRI
     VQEARTMNDF GMMNQTNYSI LPDEDGYTQS SQLLPSDRFI GPSSQPTPKW RPALYNIDSV
     DVQTGMLQPN SQWDLVQKFR KQLSEMFEDP SLQQELGKVS YQELIQQATN ELKKEHTDKI
     QIVSKLIQGS ESLADTDVNK IFLFHETVIT GLNLLSAIYV LLNTFRNNIK ALDLDTIQKS
     IIEWLRETQA ANVNRANLID WLGRRHGDIS EIRNPGLVIK ANDARLSEVY PDPTTDATAP
     LDRNLVTETL FAWFTRFVGI PADGAVRPEQ ELAARYLVDN QRIMQLLLTN IFEMTSSFNK
     LVQVRFPETS TAHVHLDFTG LISLIDSLMA DTKYFLDLLR PHIDKNIIQY YENRSNPGSF
     YWLEEHLIDK LIKPPTDAGG RPLPGGELGL EGVNQIINKT YILLTKPYNV LQLRGGAQRG
     NAANIQINNN PEFSERYEQY GRVFSRLVFY DALIENSGLR VEQVALGDFR LSNLIRTNNA
     QEENALSFWT AVAPRAYANV NDAANNLRRY RLYGSDYGIR NNRSMMMVFN QLVASYIARF
     YDAPSGKIYL NLINTFANGN FSQAVMELGY AHPDLARDNT AFGHRGDPTE QSVLLLSLGL
     MLQRLIKDTN RQGLSQHLIS TLTEIPIYLK ENYRANLPLF NKMFNILISQ GELLKQFIQY
     TKVQLARPNL TALLGANNDS IIYYNNNNVP NTGLTVGQAA LRGIGSVFRP DITLMPLGNA
     QNNTNDVVRK RLIAVINGII RGSLTLANSA MEVLHELTDH PIYFETEEHF IQNYMSRYNK
     EPLMPFSLSL YYLRDLRIEN NEVYDPLLYP NLESGSPEFK ILYGTRKLLG NDPVQLSDMP
     GVQLIMKNYN ETVVAREQIT PTRFEHFYIH AIQALRFIIN IRSFKTVMTY NENTFGGVNL
     IGEDRDDKPI ITEGIGMNAV YSLRKTLQDV ISFVESSYQE EQINNIHKIV SPRSQTRSLG
     SNRERERIFN LFDMNIMPIN VNALMRSIPL ANIYNYDYSF EEIACLMYGI SAEKVRSLDT
     AAPQPDVAQV LNIPNRPPMN TREFMLKLLI NPYVTVSITQ YGNELLFRGN AGYMSRIFRG
     DNALNMGRPK FLSDQIFNKV LFGSLYPTQF DYDEAGPGLA AGIQRGREQW GQPLSDYINQ
     ALHELVRTIR IIPQNIRVLR NIMVKNQLIA DLAAIREQLV RMRREVENMV QTPEIQNNPT
     PEVIAAAQTW TQQYRARVDF LINFIGNAQQ PNSLIQLIQN ITPLTVRAQL TTVFIRHGLP
     VPDPDQALQT DDEATQWFMT NIINQPITMI IPFTDLADDL RIFLETMERY VFNVPRWLGP
     STGRVARVPV NMAPGNIRYR TSYTENNVLT YIAEQNQEEG PWSIVKQVGV GIQKPALIQI
     GKDRFDTRLI RNLIFITNIQ RLLRLRLNLE LSQFRNVLVS PNHIINPSIT EYGFSITGPS
     ETFSDKQYDS DIRIL