POLG_PPVEA
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 03-AUG-2022, entry version 127.
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; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; 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: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
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. {ECO:0000250|UniProtKB:P04517}.
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; Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- SUBUNIT: [Viral genome-linked protein]: Interacts with host eIF4E
CC protein (via cap-binding region); this interaction mediates the
CC translation of the VPg-viral RNA conjugates (By similarity). Part of a
CC complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction
CC mediates the translation of the VPg-viral RNA conjugates (By
CC similarity). {ECO:0000250|UniProtKB:P18247}.
CC -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus
CC {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins
CC in the host nucleus. {ECO:0000250|UniProtKB:P21231}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC -!- PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes
CC post-translational proteolytic processing by the main proteinase NIa-
CC pro resulting in the production of at least ten individual proteins.
CC The P1 proteinase and the HC-pro cleave only their respective C-termini
CC autocatalytically. 6K1 is essential for proper proteolytic separation
CC of P3 from CI (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; X56258; CAA39698.1; -; mRNA.
DR PIR; PQ0221; PQ0221.
DR MEROPS; C04.001; -.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
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:0019048; P:modulation by virus of host process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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 SUPFAM; SSF56672; SSF56672; 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; Host nucleus;
KW Host-virus interaction; Hydrolase; Nucleotide-binding;
KW 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 REGION 1239..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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|UniProtKB:P09814"
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
