ID   POLG_PVYN               Reviewed;        3063 AA.
AC   P18247; Q85266; Q85267; Q85268; Q85269; Q85270; Q85271; Q85272; Q85273;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
DE   Contains:
DE     RecName: Full=Protein P3;
DE   Contains:
DE     RecName: Full=6 kDa protein 1;
DE              Short=6K1;
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     AltName: Full=NIa-pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-b;
DE              Short=NIb;
DE              EC=2.7.7.48;
DE     AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
OS   Potato virus Y (strain N) (PVY).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus; Potato virus Y.
OX   NCBI_TaxID=12219;
OH   NCBI_TaxID=4071; Capsicum (peppers).
OH   NCBI_TaxID=4085; Nicotiana.
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2732709; DOI=10.1099/0022-1317-70-4-935;
RA   Robaglia C., Durand-Tardif M., Tronchet M., Boudazin G.,
RA   Astier-Manifacier S., Casse-Delbart F.;
RT   "Nucleotide sequence of potato virus Y (N Strain) genomic RNA.";
RL   J. Gen. Virol. 70:935-947(1989).
RN   [2]
RP   SEQUENCE REVISION.
RA   Durand-Tardif M.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION (HELPER COMPONENT PROTEINASE).
RX   PubMed=10570213; DOI=10.1073/pnas.96.24.14147;
RA   Voinnet O., Pinto Y.M., Baulcombe D.C.;
RT   "Suppression of gene silencing: a general strategy used by diverse DNA and
RT   RNA viruses of plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14147-14152(1999).
RN   [4]
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).
RN   [5]
RP   FUNCTION (VIRAL GENOME-LINKED PROTEIN), AND INTERACTION WITH HOST CAPSICUM
RP   ANNUUM EIF4E1 (VIRAL GENOME-LINKED PROTEIN).
RC   STRAIN=LYE84, and SON41;
RX   PubMed=18182024; DOI=10.1111/j.1365-313x.2008.03407.x;
RA   Charron C., Nicolai M., Gallois J.-L., Robaglia C., Moury B., Palloix A.,
RA   Caranta C.;
RT   "Natural variation and functional analyses provide evidence for co-
RT   evolution between plant eIF4E and potyviral VPg.";
RL   Plant J. 54:56-68(2008).
RN   [6]
RP   INTERACTION WITH HOST TOMATO EIF4E1 AND EIF4E2 (VIRAL GENOME-LINKED
RP   PROTEIN).
RC   STRAIN=LYE84, and LYE90;
RX   PubMed=22242134; DOI=10.1371/journal.pone.0029595;
RA   Mazier M., Flamain F., Nicolai M., Sarnette V., Caranta C.;
RT   "Knock-down of both eIF4E1 and eIF4E2 genes confers broad-spectrum
RT   resistance against potyviruses in tomato.";
RL   PLoS ONE 6:e29595-e29595(2011).
RN   [7]
RP   FUNCTION (VIRAL GENOME-LINKED PROTEIN), AND VARIANTS SER-1958 AND VAL-1982.
RC   STRAIN=LYE90, N605, and SON41;
RX   PubMed=27655175; DOI=10.1099/jgv.0.000609;
RA   Lebaron C., Rosado A., Sauvage C., Gauffier C., German-Retana S., Moury B.,
RA   Gallois J.-L.;
RT   "A new eIF4E1 allele characterized by RNAseq data mining is associated with
RT   resistance to potato virus Y in tomato albeit with a low durability.";
RL   J. Gen. Virol. 97:3063-3072(2016).
RN   [8]
RP   REVIEW.
RX   PubMed=28199446; DOI=10.1590/1678-4685-gmb-2016-0092;
RA   Machado J.P.B., Calil I.P., Santos A.A., Fontes E.P.B.;
RT   "Translational control in plant antiviral immunity.";
RL   Genet. Mol. Biol. 40:292-304(2017).
RN   [9] {ECO:0007744|PDB:6NFW}
RP   STRUCTURE BY NMR OF 47-230, FUNCTION (VIRAL GENOME-LINKED PROTEIN),
RP   INTERACTION WITH HOST EIF4E (VIRAL GENOME-LINKED PROTEIN), MUTAGENESIS OF
RP   ASP-1954; GLU-1957; MET-1958 AND GLN-1959, AND IDENTIFICATION IN A COMPLEX
RP   WITH RNA; HOST EIF4E AND EIF4G (VIRAL GENOME-LINKED PROTEIN).
RX   PubMed=31712417; DOI=10.1073/pnas.1904752116;
RA   Coutinho de Oliveira L., Volpon L., Rahardjo A.K., Osborne M.J.,
RA   Culjkovic-Kraljacic B., Trahan C., Oeffinger M., Kwok B.H., Borden K.L.B.;
RT   "Structural studies of the eIF4E-VPg complex reveal a direct competition
RT   for capped RNA: Implications for translation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:24056-24065(2019).
CC   -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC       dipeptide at its own C-terminus. Interacts with virions and aphid
CC       stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC       known as post-transcriptional gene silencing (PTGS), a mechanism of
CC       plant viral defense that limits the accumulation of viral RNAs. May
CC       have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.
CC   -!- FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It
CC       may be involved in replication.
CC   -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC       {ECO:0000250|UniProtKB:P13529}.
CC   -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC       {ECO:0000250|UniProtKB:P09814}.
CC   -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC       EIF4E-dependent translation of viral genomic RNAs (PubMed:31712417).
CC       Binds to the cap-binding site of host EIF4E and thus interferes with
CC       the host EIF4E-dependent mRNA export and translation (PubMed:31712417).
CC       VPg-RNA directly binds EIF4E and is a template for transcription
CC       (PubMed:31712417). Also forms trimeric complexes with EIF4E-EIF4G,
CC       which are templates for translation (PubMed:31712417).
CC       {ECO:0000269|PubMed:31712417}.
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=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   -!- 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=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC         the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC         potyviral polyprotein.; EC=3.4.22.45;
CC         Evidence={ECO:0000250|UniProtKB:P04517};
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 (PubMed:31712417). Part of
CC       a complex that comprises VPg, RNA, host EIF4E and EIF4G; this
CC       interaction mediates the translation of the VPg-viral RNA conjugates
CC       (PubMed:31712417). Interaction is possible in susceptible hosts but
CC       impaired in resistant plants: the VPg of strain LYE84 interacts with
CC       tomato eIF4E1 and eIF4E2 as well as with the Capsicum annuum eIF4E1
CC       susceptible allele pvr2(+) but not with resistant alleles pvr2(1),
CC       pvr2(2), pvr2(3), pvr2(4), pvr2(5), pvr2(6), pvr2(7), pvr2(8) and
CC       pvr2(9), the VPg of strain SON41 interacts with C.annuum eIF4E1
CC       susceptible alleles pvr2(+), pvr2(1), pvr2(2), pvr2(3) and pvr2(4) but
CC       not with resistant alleles pvr2(5), pvr2(6), pvr2(7), pvr2(8) and
CC       pvr2(9), the VPg of strain LYE90 interacts only with tomato eIF4E1
CC       (PubMed:22242134, PubMed:18182024). {ECO:0000269|PubMed:18182024,
CC       ECO:0000269|PubMed:22242134, ECO:0000269|PubMed:31712417}.
CC   -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle.
CC       Note=Probably colocalizes with 6K2-induced vesicles associated with
CC       host chloroplasts. {ECO:0000250|UniProtKB:P13529}.
CC   -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with
CC       host chloroplasts. {ECO:0000250|UniProtKB:P09814}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=P18247-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ93-1; Sequence=External;
CC   -!- DOMAIN: [Helper component proteinase]: The N-terminus is involved in
CC       interaction with stylets. The central part is involved in interaction
CC       with virions and the C-terminus is involved in cell-to cell movement of
CC       the virus.
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]: Potyviral RNA is expressed as two
CC       polyproteins which undergo post-translational proteolytic processing.
CC       Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases
CC       resulting in the production of at least ten individual proteins. P3N-
CC       PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC       the production of three individual proteins. The P1 proteinase and the
CC       HC-pro cleave only their respective C-termini autocatalytically. 6K1 is
CC       essential for proper proteolytic separation of P3 from CI (By
CC       similarity). {ECO:0000250}.
CC   -!- POLYMORPHISM: [Viral genome-linked protein]: Variant of the resistance-
CC       breaking strain SON41 has the ability to contaminate Capsicum annuum
CC       plants containing resistant alleles pvr2(+), pvr2(1), pvr2(2), pvr2(3)
CC       and pvr2(4) but not plants containing alleles pvr2(5), pvr2(6),
CC       pvr2(7), pvr2(8) and pvr2(9). {ECO:0000269|PubMed:18182024}.
CC   -!- POLYMORPHISM: [Viral genome-linked protein]: Variant of the resistance-
CC       breaking strain LYE84 has the ability to contaminate Capsicum annuum
CC       plants containing the resistant allele pvr2(+) but not plants
CC       containing alleles pvr2(1), pvr2(2), pvr2(3), pvr2(4), pvr2(5),
CC       pvr2(6), pvr2(7), pvr2(8) and pvr2(9). {ECO:0000269|PubMed:18182024}.
CC   -!- POLYMORPHISM: [Viral genome-linked protein]: Variant of the resistance-
CC       breaking strain SON41g has the ability to contaminate Solanum
CC       pimpinellifolium cv. LA0411 plants containing the resistant allele
CC       eIF4E1-pot1(2). {ECO:0000269|PubMed:27655175}.
CC   -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC       translation.
CC   -!- MISCELLANEOUS: VPg is not an intrinsically disordered protein.
CC       {ECO:0000269|PubMed:31712417}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X12456; CAA30988.1; -; Genomic_RNA.
DR   EMBL; D00441; BAA00342.1; -; Genomic_RNA.
DR   PIR; JS0166; JS0166.
DR   RefSeq; NP_056759.1; NC_001616.1.
DR   PDB; 6NFW; NMR; -; A=47-230.
DR   PDBsum; 6NFW; -.
DR   SMR; P18247; -.
DR   MEROPS; C04.002; -.
DR   MEROPS; C06.001; -.
DR   KEGG; vg:1494052; -.
DR   BRENDA; 3.4.22.45; 5005.
DR   Proteomes; UP000000520; Segment.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.90.70.150; Helper component proteinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
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; IPR039560; Potyvirid-P3.
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   PANTHER; PTHR43519; ATP-DEPENDENT RNA HELICASE HRPB; 1.
DR   PANTHER; PTHR43519:SF1; ATP-DEPENDENT RNA HELICASE HRPB; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW   Helical capsid protein; Helicase; Host cytoplasmic vesicle; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW   Suppressor of RNA silencing; Thiol protease; Transferase;
KW   Viral immunoevasion; Viral RNA replication; Virion.
FT   CHAIN           1..3063
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420017"
FT   CHAIN           1..284
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040407"
FT   CHAIN           285..740
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040408"
FT   CHAIN           741..1105
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040409"
FT   CHAIN           1106..1157
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040410"
FT   CHAIN           1158..1791
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040411"
FT   CHAIN           1792..1843
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040412"
FT   CHAIN           1844..2031
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040413"
FT   CHAIN           2032..2275
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040414"
FT   CHAIN           2276..2796
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040415"
FT   CHAIN           2797..3063
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040416"
FT   DOMAIN          141..284
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          618..740
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1229..1381
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1400..1559
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2032..2250
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2519..2643
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          1949..1964
FT                   /note="Interaction with host EIF4E"
FT                   /evidence="ECO:0000305|PubMed:31712417"
FT   REGION          2798..2841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           334..337
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           592..594
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1331..1334
FT                   /note="DECH box"
FT   MOTIF           1884..1892
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2812..2841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        192
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        201
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        235
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        626
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        699
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2077
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2112
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2182
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   BINDING         1242..1249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   SITE            284..285
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            740..741
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1105..1106
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1157..1158
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1791..1792
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1843..1844
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1907
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000269|PubMed:31712417"
FT   SITE            1949
FT                   /note="Interaction with host EIF4E"
FT                   /evidence="ECO:0000269|PubMed:31712417"
FT   SITE            2031..2032
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2275..2276
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2796..2797
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1907
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09814"
FT   VARIANT         1944
FT                   /note="S -> G (in strain: SON41)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1948
FT                   /note="K -> R (in strain: SON41)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1958
FT                   /note="M -> P (in strain: SON41)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1958
FT                   /note="M -> S (in strain: SON41g)"
FT                   /evidence="ECO:0000269|PubMed:27655175"
FT   VARIANT         1962
FT                   /note="G -> R (in strain: LYE84)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1962
FT                   /note="G -> Y (in strain: SON41)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1966
FT                   /note="T -> N (in strain: LYE84)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1966
FT                   /note="T -> S (in strain: SON41)"
FT                   /evidence="ECO:0000269|PubMed:18182024"
FT   VARIANT         1982
FT                   /note="I -> V (in strain: SON41g)"
FT                   /evidence="ECO:0000269|PubMed:27655175"
FT   MUTAGEN         1954
FT                   /note="D->K: Reduced binging to host EIF4E; when associated
FT                   with K-114 and K-116."
FT                   /evidence="ECO:0000269|PubMed:31712417"
FT   MUTAGEN         1957
FT                   /note="E->K: Reduced binging to host EIF4E; when associated
FT                   with K-111 and K-116."
FT                   /evidence="ECO:0000269|PubMed:31712417"
FT   MUTAGEN         1958
FT                   /note="M->A: Reduced binging to host EIF4E; when associated
FT                   with K-116."
FT                   /evidence="ECO:0000269|PubMed:31712417"
FT   MUTAGEN         1959
FT                   /note="Q->K: Reduced binging to host EIF4E; when associated
FT                   with A-115. Reduced binging to host EIF4E; when associated
FT                   with K-111 and K-114."
FT                   /evidence="ECO:0000269|PubMed:31712417"
FT   STRAND          1916..1920
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   STRAND          1922..1924
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   STRAND          1928..1930
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   HELIX           1936..1953
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   TURN            1959..1962
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   STRAND          1967..1972
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   STRAND          1978..1984
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   STRAND          1995..1997
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   STRAND          2016..2019
FT                   /evidence="ECO:0007829|PDB:6NFW"
FT   TURN            2020..2022
FT                   /evidence="ECO:0007829|PDB:6NFW"
SQ   SEQUENCE   3063 AA;  347539 MW;  3EC79125DE33F1BB CRC64;
     MATYMSTICF GSFECKLPYS PASCEHIVKE REVPASVDPF ADLETQLSAR LLKQKYATVR
     VLKNGTFTYR YKTDAQIMRI QKKLERKDRE EYHFQMAAPS IVSKITIAGG DPPSKSEPQA
     PRGIIHTTPR MRKVKTRPII KLTEGQMNHL IKQIKQIMSE KRGSVHLISK KTTHVQYKKI
     LGAYSAAVRT AHMMGLRRRV DFRCDMWTVG LLQRLARTDK WSNQVRTINI RRGDSGVILN
     TKSLKGHFGR SSGGLFIVRG SHEGKLYDAR SRVTQSILNS MIQFSNADNF WKGLDGNWAR
     MRYPSDHTCV AGLPVEDCGR VAALMAHSIL PCYKITCPTC AQQYASLPVS DLFKLLHKHA
     RDGLNRLGAD KDRFIHVNKF LIALEHLTEP VDLNLELFNE IFKSIGEKQQ APFKNLNVLN
     NFFLKGKENT AHEWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
     NQLDKNANFL WGQREYHAKR FFSNFFEEID PAKGYSAYEI RKHPSGTRKL SIGNLVVPLD
     LAEFRQKMKG DYRKQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG
     NSGDQKFVDL PKGDSEMLYI AKQGYCYINV FLAMLINISE EDAKDFTKKV RDMCVPKLGT
     WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV VDSFGSQTTG YHILKASSVS
     QLILFANDEL ESDIKHYRVG GVPNASPELG STISPFREGG VIMSESAALK LLLKGIFRPK
     VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
     SAAETLVAQR IIIDAAATDL LDATCDGFNL HLTYPTALMV LQVVKNRNEC DDTLFKAGFP
     SYNTSVVQIM EKNYLNLLND AWKDLTWREN YPQHGTHTEQ NALSTRYIKP TEKADLKGLY
     NISPQAFLGR SAQVVKGTAS GLSERFNNYF NTKCVNISSF FIRRIFRRLP TFVTFVNSLL
     VISMLTSVVA VCQAIILDQR KYRREIELMQ IEKNEIVCME LYASLQRKLE RDFTWDEYIE
     YLKSVNPQIV QFAQAQMEEY DVRHQRSTPV VKNLEQVVAF MALVIMVFDA ERSDCVFKTL
     NKFKGVLSSL DYEVRHQSLD DVIKNFDERN EIIDFELSED TIRTSSVLDT KFSDWWDRQI
     QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST GLPVHLSVAG
     SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSIFGS SPISVMTSGF ALHYFANNRS
     QLAQFNFVIF DECHVLDPSA MAFRSLLSVY HQACKVLKVS ATPVGREVEF TTQQPVKLIV
     EDTVSFQSFV DAQGSKTNAD VVQFGSNVLV YVSSYNEVDT LAKLLTDKNM MVTKVDGRTM
     KHGCLEIVTK GTSARPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKVS
     VSYGERIQRL GRVGRFKKGV ALRIGHTEKG IIEIPSMVAT EAALACFAYN LPVMTGGVST
     SLIGNCTVRQ VKTMQQFELS PFFIQNFVAH DGSMHPVIHD ILKKYKLRDC MTPLCDQSIP
     YRASSTWLSV SEYERLGVAL EIPKQVKIAF HIKEIPPKLH EMLWETVVKY KDVCLFPSIR
     ASSISKIAYT LRTDLFAIPR TLILVERLLE EERVKQSQFR SLIDEGCSSM FSIVNLTNTL
     RARYAKDYTA ENIQKLEKVR SQLKEFSNLD GSACEENLIK RYESLQFVHH QAATSLAKDL
     KLKGIWNKSL VAKDLIIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR IQALKFRHAR
     DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS RRFINMYGFD PTEYSFIQFV
     DPLTGRQIEE NVYADIRDIQ ERFSEVRKKM VENDDIEMQA LGSNTTIHAY FRKDWCDKAL
     KIDLMPHNPL KVCDKTNGIA KFPERELELR QTGPAVEVDV KDIPAQEVEH EAKSLMRGLR
     DFNPIAQTVC RLKVSVEYGA SEMYGFGFGA YIVANHHLFR SYNGSMEVQS MHGTFRVKNL
     HSLSVLPIKG RDIILIKMPK DFPVFPQKLH FRAPTQNERI CLVGTNFQEK YASSIITETS
     TTYNIPGSTF WKHWIETDNG HCGLPVVSTA DGCIVGIHSL ANNAHTTNYY SAFDEDFESK
     YLRTNEHNEW VKSWVYNPDT VLWGPLKLKD STPKGLFKTT KLVQDLIDHD VVVEQAKHSA
     WMFEALTGNL QAVATMKSQL VTKHVVKGEC RHFTEFLTVD AEAEAEAFFR PLMDAYGKSL
     LNRDAYIKDI MKYSKPIDVG VVDRMHLRKP SIGLSSTCNV HGFKKCAYVT DEQEIFKALN
     MKAAVGASYG CKKKDYFEHF TDADKEEIVM QSCLRLYKGL LGIWNGSLKA ELRCKEKILA
     NKTRTFTAAP LDTLLGGKVC VDDFNNQFYS KNIECCWTVG MTKFYGGWDK LLRRLPENWV
     YCDADGSQFD SSLTPYLINA VLTIRSTYME DWDVGLQMLR NLYTEIVYTP ISTPDGTIVK
     KFRGNNSGQP STVVDNSLMV VLAMHYALIK ECVEFEEIDS TCVFFVNGDD LLIAVNPEKE
     SILDRMSQHF SDLGLNYDFS SRTRRKEELW FMSHRGLLIE GMYVPKLEEE RIVSILQWDR
     ADLPEHRLEA ICAAMIESWG YSELTHQIRR FYSWLLQQQP FATIAQEGKA PYIASMALRK
     LYMDRAVDEE ELRAFTEMMV ALDDEFELDS YEVHHQANDT IDAGGSNKKD AKPEQGSIQP
     NPNKGKDKDV NAGTSGTHTV PRIKAITSKM RMPTSKGATV PNLEHLLEYA PQQIDISNTR
     ATQSQFDTWY EAVRMAYDIG ETEMPTVMNG LMVWCIENGT SPNVNGVWVM MDGNEQVEYP
     LKPIVENAKP TLRQIMAHFS DVAEAYIEMR NKKEPYMPRY GLIRNLRDMG LARYAFDFYE
     VTSRTPVRAR EAHIQMKAAA LKSAQPRLFG LDGGISTQEE NTERHTTEDV SPSMHTLLGV
     KNM
//