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Database: UniProt
Entry: Q01681
LinkDB: Q01681
Original site: Q01681 
ID   POLG_PPVEA              Reviewed;        1518 AA.
AC   Q01681;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   11-DEC-2019, entry version 118.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Cytoplasmic inclusion protein;
DE              Short=CI;
DE              EC=3.6.4.-;
DE   Contains:
DE     RecName: Full=6 kDa protein 2;
DE              Short=6K2;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein A;
DE              Short=NI-A;
DE              Short=NIA;
DE              EC=3.4.22.44;
DE     AltName: Full=49 kDa proteinase;
DE              Short=49 kDa-Pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-B;
DE              Short=NIB;
DE     AltName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
DE   Flags: Fragment;
OS   Plum pox potyvirus (strain El amar) (PPV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31738;
OH   NCBI_TaxID=36596; Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OH   NCBI_TaxID=36595; Prunus cerasifera (cherry plum).
OH   NCBI_TaxID=3758; Prunus domestica (Garden plum).
OH   NCBI_TaxID=105665; Prunus glandulosa.
OH   NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH   NCBI_TaxID=88123; Prunus salicina.
OH   NCBI_TaxID=114937; Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1856701; DOI=10.1099/0022-1317-72-7-1741;
RA   Wetzel T., Candresse T., Ravelonandro M., Delbos R.P., Mazyad H.,
RA   Aboul-Ata A.E., Dunez J.;
RT   "Nucleotide sequence of the 3'-terminal region of the RNA of the El Amar
RT   strain of plum pox potyvirus.";
RL   J. Gen. Virol. 72:1741-1746(1991).
RN   [2]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
CC   -!- FUNCTION: [Capsid protein]: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in the
CC       regulation of viral RNA amplification.
CC   -!- FUNCTION: [Nuclear inclusion protein B]: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC   -!- FUNCTION: [Cytoplasmic inclusion protein]: has helicase activity. It
CC       may be involved in replication.
CC   -!- FUNCTION: [Nuclear inclusion protein A]: has RNA-binding and
CC       proteolytic activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that vary
CC         with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC         Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC         the viral polyprotein, but other proteins and oligopeptides
CC         containing the appropriate consensus sequence are also cleaved.;
CC         EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC       to the 5'-end of the genomic RNA. This uridylylated form acts as a
CC       nucleotide-peptide primer for the polymerase (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Genome polyprotein of potyviruses undergoes post-translational
CC       proteolytic processing by the main proteinase NIa-pro resulting in the
CC       production of at least ten individual proteins. The P1 proteinase and
CC       the HC-pro cleave only their respective C-termini autocatalytically.
CC       6K1 is essential for proper proteolytic separation of P3 from CI (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; X56258; CAA39698.1; -; mRNA.
DR   PIR; PQ0221; PQ0221.
DR   PRIDE; Q01681; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   2: Evidence at transcript level;
KW   Capsid protein; Covalent protein-RNA linkage; Hydrolase;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW   RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN           <1..179
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040325"
FT   CHAIN           1..1518
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420006"
FT   CHAIN           180..232
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040326"
FT   CHAIN           233..425
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040327"
FT   CHAIN           426..668
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040328"
FT   CHAIN           669..1186
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040329"
FT   CHAIN           1187..1518
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040330"
FT   DOMAIN          426..644
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          910..1034
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   MOTIF           273..280
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        471
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        506
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        576
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            179..180
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            232..233
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            425..426
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            668..669
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1186..1187
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         295
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   1518 AA;  172033 MW;  A1268F972F5B247C CRC64;
     LNKLAIPNAN VCGWMSVRDY KRQGCNLDLD DNIRVPFYVK DLPETLHEKI WQTVEAHKAD
     AGFGRICSSS ACKIAYTLQT DIHSIPRTVK ILDALLEQER TKQAHFRSMT SQSCSSSNFS
     LSSITSAIRS KYAKDHTEEN IGVLQMAKAQ LLEFKNLNID PSYPELVRNF GALECVHHQT
     KEGVSKALRL KGHWNKQLVT RDATLMLGVL GGGAWMIFSY LRDSFKEEVV HQGFNRRQRQ
     KLKFRQARDN RMAREVYGDD STMEDYFGSA YSKKGKSKGR TRGMGTKTRK FVNMYGYDPT
     DYNFVRFVDP LTGHTLDENP LMDINLVQEH FSQVRNDYLG DDKITMQHIM SNPGIVAYYI
     KDATQKALKV DLTPHNPLRV CDKTATIAGF PEREFELRQT GQPVLVEPNA IPQINEEGDE
     EVGHESKSLF RGLRDYNPIA SSICHLTNAS GTRQSEIYGL GFGGLIVTNQ HLFKRNDGEL
     TIRSHHGEFV VKDTKTLKLL PCKGRDIIII RLPKDFPPFP RRLQFRTPTA EDRVCLIGSN
     FQTKSVSSTM SETSATYPVD NSHFWKHWIS TKDGHCGLPI VSTRDGSILG LHSLANSTNT
     QNFYAAFPDN FETTYLANQD NDNWIKQWRY NPDEVCWGSL QLKRDVPQSP FTICKLLTDL
     DGEFVYNQAK TTHWLRDKLE GNLKAVGACP GQLVTKHVVK GKCTLFETYL LTHPEEREFF
     QPLMGAYQKS ALNKDAYVKD LMKYSKSIVV GAVDCEQFER AVDVVISMLI SKGFSECSYV
     TDPEEIFSAL NMKAAVGALY SGKKRDYFKD TSELEKEEFV RASCKRLFMG KKGVWNGSLK
     AELRPKEKVE ANKTRSFTAA PIDTLLGGKV CVDDFNNQFY SLNLHCPWSV GMTKFRGGWD
     KLLRALPDGW IYCDADGSQF DSSLSPYLIN AVLNIRLAFM EEWDIGEQML SNLYTEIVYT
     PIATPDGTIV KKFKGNNSGQ PSTVVDNTLM VILAMTYSLL KLGYHPDTHE CICRYFVNGD
     DLVLAVHPAY ESIYDELQHH FSQLGLNYTF TTKTENKEDL WFMSHKGIMC EGMYIPKLEP
     ERIVSILEWD RSSEPIHRLE AICASMVEAW GYKELLREIR KFYSWVLEQA PYNALSKDGK
     APYIAETALK KLYTDTEASE TEIERYLEAF YSNLTDEDES NVVVHQADEK EDDEEEVDAG
     RPLVTTTQQP IVTTTTQQTP ITSTTLQATQ AMFNPIFTPA TTEPTTRTVP HTTTTTPPSF
     GVIGNEDTAP NASNAVVRTG RDRDVDAGSI GTFTVPRLKA MTSKLSLPKV KGKAIMNLNH
     LAFYSPAQVD LSNTRAPQSC FQTWYEGVRR DYDVTDDEMS IILNGLMVWC IENGTSPNIN
     GMWVMMDGET QVEYPIKPLL DHAKPTFRQI MAHFSNVAEA YIEKRNYEKA YMPRYGIQRN
     LTDYSLARYA FDFYEMTSTT PVRAREAHIQ MKAAALRNAQ NRLFGLDGNV GTQEEDTERH
     TAGDVNRNMH NLLGMRGV
//
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