POLG_TEV
ID POLG_TEV Reviewed; 3054 AA.
AC P04517; Q88500; Q88501; Q88502; Q88504; Q88505; Q88506; Q89773;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000269|PubMed:1962435};
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:0000269|PubMed:2656254, ECO:0000269|PubMed:2688301};
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 {ECO:0000269|PubMed:2475971};
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 Tobacco etch virus (TEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12227;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=53851; Cassia.
OH NCBI_TaxID=4076; Datura stramonium (Jimsonweed) (Common thornapple).
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH NCBI_TaxID=24663; Physalis.
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Allison R., Johnston R.E., Dougherty W.G.;
RT "The nucleotide sequence of the coding region of tobacco etch virus genomic
RT RNA: evidence for the synthesis of a single polyprotein.";
RL Virology 154:9-20(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2344-3054.
RX PubMed=16593574; DOI=10.1073/pnas.82.12.3969;
RA Allison R.F., Sorenson J.C., Kelly M.E., Armstrong F.B., Dougherty W.G.;
RT "Sequence determination of the capsid protein gene and flanking regions of
RT tobacco etch virus: evidence for synthesis and processing of a polyprotein
RT in potyvirus genome expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3969-3972(1985).
RN [3]
RP CATALYTIC ACTIVITY (HELPER COMPONENT PROTEINASE), FUNCTION (HELPER
RP COMPONENT PROTEINASE), AND PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX PubMed=2656254; DOI=10.1002/j.1460-2075.1989.tb03386.x;
RA Carrigton J.C., Cary S.M., Parks T.D., Dougherty W.G.;
RT "A second proteinase encoded by a plant potyvirus genome.";
RL EMBO J. 8:365-370(1989).
RN [4]
RP ACTIVE SITES (HELPER COMPONENT PROTEINASE), MUTAGENESIS OF SER-610;
RP HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675; ASP-689; CYS-694;
RP SER-698; ASP-715; HIS-716; HIS-722; ASP-725; SER-726; SER-729; HIS-735;
RP SER-743 AND SER-755, AND CATALYTIC ACTIVITY (HELPER COMPONENT PROTEINASE).
RX PubMed=2688301; DOI=10.1016/0042-6822(89)90582-5;
RA Oh C.-S., Carrington J.C.;
RT "Identification of essential residues in potyvirus proteinase HC-Pro by
RT site-directed mutagenesis.";
RL Virology 173:692-699(1989).
RN [5]
RP ACTIVE SITES (NUCLEAR INCLUSION PROTEIN A), CATALYTIC ACTIVITY (NUCLEAR
RP INCLUSION PROTEIN A), AND FUNCTION (NUCLEAR INCLUSION PROTEIN A).
RX PubMed=2475971; DOI=10.1016/0042-6822(89)90132-3;
RA Dougherty W.G., Parks T.D., Cary S.M., Bazan J.F., Fletterick R.J.;
RT "Characterization of the catalytic residues of the tobacco etch virus 49-
RT kDa proteinase.";
RL Virology 172:302-310(1989).
RN [6]
RP ACTIVE SITES (P1 PROTEINASE), AND MUTAGENESIS OF HIS-214 AND SER-256.
RX PubMed=1962435; DOI=10.1016/0042-6822(91)90522-d;
RA Verchot J., Koonin E.V., Carrington J.C.;
RT "The 35-kDa protein from the N-terminus of the potyviral polyprotein
RT functions as a third virus-encoded proteinase.";
RL Virology 185:527-535(1991).
RN [7]
RP FUNCTION (HELPER COMPONENT PROTEINASE), AND MUTAGENESIS OF PHE-314 AND
RP LYS-358.
RX PubMed=9880030; DOI=10.1099/0022-1317-79-12-3119;
RA Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C., Baker J.,
RA Pirone T.P.;
RT "Mutations in the potyvirus helper component protein: effects on
RT interactions with virions and aphid stylets.";
RL J. Gen. Virol. 79:3119-3122(1998).
RN [8]
RP FUNCTION (HELPER COMPONENT PROTEINASE).
RX PubMed=11414807; DOI=10.1006/viro.2001.0901;
RA Kasschau K.D., Carrington J.C.;
RT "Long-distance movement and replication maintenance functions correlate
RT with silencing suppression activity of potyviral HC-Pro.";
RL Virology 285:71-81(2001).
RN [9]
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 [10]
RP INTERACTION WITH HOST EIF4E1 (VIRAL GENOME-LINKED PROTEIN).
RC STRAIN=HAT, and NW;
RX PubMed=15842624; DOI=10.1111/j.1365-313x.2005.02381.x;
RA Kang B.-C., Yeam I., Frantz J.D., Murphy J.F., Jahn M.M.;
RT "The pvr1 locus in Capsicum encodes a translation initiation factor eIF4E
RT that interacts with Tobacco etch virus VPg.";
RL Plant J. 42:392-405(2005).
RN [11]
RP VARIANTS LEU-1960; ASP-1961; HIS-1962 AND ASP-1964, AND INTERACTION WITH
RP HOST EIF4E1 (VIRAL GENOME-LINKED PROTEIN).
RC STRAIN=CAA10, and HAT;
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 [12]
RP FUNCTION (VIRAL GENOME-LINKED PROTEIN).
RC STRAIN=HAT;
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 [13]
RP FUNCTION (VIRAL GENOME-LINKED PROTEIN).
RC STRAIN=CAA10, HAT, and S103;
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 [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2038-2794, SUBUNIT (NUCLEAR
RP INCLUSION PROTEIN A), DISULFIDE BOND (NUCLEAR INCLUSION PROTEIN A), AND
RP MUTAGENESIS OF CYS-2188.
RX PubMed=12377789; DOI=10.1074/jbc.m207224200;
RA Phan J., Zdanov A., Evdokimov A.G., Tropea J.E., Peters H.K. III,
RA Kapust R.B., Li M., Wlodawer A., Waugh D.S.;
RT "Structural basis for the substrate specificity of tobacco etch virus
RT protease.";
RL J. Biol. Chem. 277:50564-50572(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2038-2279, SUBUNIT, DISULFIDE BOND
RP (NUCLEAR INCLUSION PROTEIN A), AND ACTIVE SITES (NUCLEAR INCLUSION PROTEIN
RP A).
RX PubMed=15919091; DOI=10.1016/j.jmb.2005.04.013;
RA Nunn C.M., Jeeves M., Cliff M.J., Urquhart G.T., George R.R., Chao L.H.,
RA Tscuchia Y., Djordjevic S.;
RT "Crystal structure of tobacco etch virus protease shows the protein C
RT terminus bound within the active site.";
RL J. Mol. Biol. 350:145-155(2005).
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 (PubMed:2656254). Interacts with
CC virions and aphid stylets (PubMed:9880030). Acts as a suppressor of
CC RNA-mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs (PubMed:11414807). May have RNA-binding
CC activity. {ECO:0000269|PubMed:11414807, ECO:0000269|PubMed:2656254,
CC ECO:0000269|PubMed:9880030}.
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 (Probable). Binds to
CC the cap-binding site of host EIF4E and thus interferes with the host
CC EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA
CC 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, ECO:0000305|PubMed:22242134,
CC ECO:0000305|PubMed:27655175}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000269|PubMed:2475971}.
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.
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:0000269|PubMed:2475971};
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 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:0000269|PubMed:2656254, ECO:0000269|PubMed:2688301};
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). Interaction is possible in susceptible hosts but impaired
CC in resistant plants: the VPg of strain HAT interacts with tomato eIF4E1
CC and eIF4E2 as well as with Capsicum annuum eIF4E1 susceptible alleles
CC pvr2(+), pvr2(3) and pvr2(9) but not with the resistant allele pvr2(2),
CC the VPg of strain CAA10 interacts with C.annuum eIF4E1 susceptible
CC alleles pvr2(+), pvr2(2), pvr2(3) and pvr2(9), the VPg of strain NW
CC interacts at least with C.annuum eIF4E1 (PubMed:15842624,
CC PubMed:18182024). {ECO:0000250|UniProtKB:P18247,
CC ECO:0000269|PubMed:15842624, ECO:0000269|PubMed:18182024}.
CC -!- SUBUNIT: [Nuclear inclusion protein A]: Homodimer; disulfide-linked.
CC {ECO:0000269|PubMed:12377789, ECO:0000269|PubMed:15919091}.
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=P04517-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK09-1; 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 CAA10 has the ability to contaminate Capsicum annuum
CC plants containing resistant alleles pvr2(+), pvr2(1), pvr2(2), pvr2(3),
CC pvr2(4), pvr2(5), pvr2(6), pvr2(7), pvr2(8) and pvr2(9).
CC {ECO:0000269|PubMed:18182024}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC translation.
CC -!- MISCELLANEOUS: [Viral genome-linked protein]: Displayed sequence is
CC strain HAT which confers the ability to contaminate Capsicum annuum
CC plants containing alleles pvr2(+), pvr2(1), pvr2(3), pvr2(4), pvr2(5),
CC pvr2(6), pvr2(7), pvr2(8) and pvr2(9) but not plants containing the
CC allele pvr2(2). {ECO:0000269|PubMed:18182024}.
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; M15239; AAA47910.1; -; Genomic_RNA.
DR EMBL; M11458; AAA47909.1; -; Genomic_RNA.
DR EMBL; M11216; AAA47908.1; ALT_SEQ; Genomic_RNA.
DR PIR; A04207; GNBVEV.
DR RefSeq; NP_062908.1; NC_001555.1. [P04517-1]
DR PDB; 1LVB; X-ray; 2.20 A; A/B=2038-2273, C/D=2785-2794.
DR PDB; 1LVM; X-ray; 1.80 A; A/B=2038-2258, C/D=2786-2794, E=2267-2273.
DR PDB; 1Q31; X-ray; 2.70 A; A/B=2038-2279.
DR PDB; 6SUQ; X-ray; 3.70 A; A=2038-2273.
DR PDBsum; 1LVB; -.
DR PDBsum; 1LVM; -.
DR PDBsum; 1Q31; -.
DR PDBsum; 6SUQ; -.
DR SMR; P04517; -.
DR MEROPS; C04.004; -.
DR MEROPS; C06.001; -.
DR PRIDE; P04517; -.
DR DNASU; 1502321; -.
DR GeneID; 1502321; -.
DR KEGG; vg:1502321; -.
DR EvolutionaryTrace; P04517; -.
DR Proteomes; UP000007404; Genome.
DR Proteomes; UP000201712; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
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-directed 5'-3' 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:0019048; P:modulation by virus of host process; IDA: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 Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR011492; DEAD_Flavivir.
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 Pfam; PF07652; Flavi_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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 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 Disulfide bond; Helical capsid protein; Helicase; Host cytoplasmic vesicle;
KW Host nucleus; Host-virus interaction; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3054
FT /note="Genome polyprotein"
FT /id="PRO_0000420026"
FT CHAIN 1..304
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040450"
FT CHAIN 305..763
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040451"
FT CHAIN 764..1110
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040452"
FT CHAIN 1111..1163
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040453"
FT CHAIN 1164..1796
FT /note="Cytoplasmic inclusion protein"
FT /id="PRO_0000040454"
FT CHAIN 1797..1849
FT /note="6 kDa protein 2"
FT /id="PRO_0000040455"
FT CHAIN 1850..2037
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040456"
FT CHAIN 2038..2279
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040457"
FT CHAIN 2280..2791
FT /note="Nuclear inclusion protein B"
FT /id="PRO_0000040458"
FT CHAIN 2792..3054
FT /note="Capsid protein"
FT /id="PRO_0000040459"
FT DOMAIN 163..304
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 641..763
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1234..1386
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1401..1564
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2038..2255
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2521..2641
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2798..2827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 358..361
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT MOTIF 615..617
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1336..1339
FT /note="DECH box"
FT MOTIF 1889..1896
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 2799..2818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219,
FT ECO:0000269|PubMed:1962435"
FT ACT_SITE 223
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 256
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219,
FT ECO:0000269|PubMed:1962435"
FT ACT_SITE 649
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 722
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2083
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000269|PubMed:2475971"
FT ACT_SITE 2118
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000269|PubMed:2475971"
FT ACT_SITE 2188
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000269|PubMed:2475971"
FT BINDING 1247..1254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 304..305
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 763..764
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080,
FT ECO:0000269|PubMed:2656254"
FT SITE 1110..1111
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1163..1164
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1796..1797
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1849..1850
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2037..2038
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2279..2280
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2791..2792
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1911
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
FT DISULFID 2167
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:12377789,
FT ECO:0000269|PubMed:15919091"
FT VARIANT 1960
FT /note="I -> L (in strain: CAA10)"
FT /evidence="ECO:0000269|PubMed:18182024"
FT VARIANT 1961
FT /note="E -> D (in strain: CAA10)"
FT /evidence="ECO:0000269|PubMed:18182024"
FT VARIANT 1962
FT /note="P -> H (in strain: CAA10)"
FT /evidence="ECO:0000269|PubMed:18182024"
FT VARIANT 1964
FT /note="S -> D (in strain: CAA10)"
FT /evidence="ECO:0000269|PubMed:18182024"
FT MUTAGEN 214
FT /note="H->A: Complete loss of proteolytic activity of P1
FT proteinase."
FT /evidence="ECO:0000269|PubMed:1962435"
FT MUTAGEN 256
FT /note="S->A: Complete loss of proteolytic activity of P1
FT proteinase."
FT /evidence="ECO:0000269|PubMed:1962435"
FT MUTAGEN 314
FT /note="F->L: Complete loss of aphid transmission."
FT /evidence="ECO:0000269|PubMed:9880030"
FT MUTAGEN 358
FT /note="K->E: Complete loss of interaction with stylet and
FT aphid transmission; no effect on virion binding."
FT /evidence="ECO:0000269|PubMed:9880030"
FT MUTAGEN 610
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 619
FT /note="H->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 625
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 627
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 632
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 649
FT /note="C->S: Complete loss of proteolytic activity of HC-
FT pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 675
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 689
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 694
FT /note="C->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 698
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 715
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 716
FT /note="H->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 722
FT /note="H->S: Complete loss of proteolytic activity of HC-
FT pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 725
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 726
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 729
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT MUTAGEN 735
FT /note="H->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 743
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 755
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 2188
FT /note="C->A: Complete loss of NIa-pro activity."
FT /evidence="ECO:0000269|PubMed:12377789"
FT HELIX 2038..2040
FT /evidence="ECO:0007829|PDB:1LVM"
FT HELIX 2049..2052
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2055..2062
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2065..2074
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2077..2080
FT /evidence="ECO:0007829|PDB:1LVM"
FT HELIX 2082..2086
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2089..2096
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2099..2104
FT /evidence="ECO:0007829|PDB:1LVM"
FT HELIX 2106..2108
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2109..2113
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2120..2123
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2145..2152
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2154..2157
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2159..2162
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2169..2171
FT /evidence="ECO:0007829|PDB:1LVM"
FT TURN 2172..2175
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2176..2179
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2191..2194
FT /evidence="ECO:0007829|PDB:1LVM"
FT TURN 2195..2197
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2200..2208
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2209..2211
FT /evidence="ECO:0007829|PDB:1Q31"
FT STRAND 2213..2218
FT /evidence="ECO:0007829|PDB:1LVM"
FT HELIX 2223..2228
FT /evidence="ECO:0007829|PDB:1LVM"
FT HELIX 2230..2232
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2235..2238
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2243..2248
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2251..2256
FT /evidence="ECO:0007829|PDB:1LVM"
FT STRAND 2276..2278
FT /evidence="ECO:0007829|PDB:1Q31"
FT STRAND 2788..2790
FT /evidence="ECO:0007829|PDB:1LVM"
SQ SEQUENCE 3054 AA; 346164 MW; 0AF9A3626960B5CE CRC64;
MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH KPVIFGEDYI
TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN NKRNRRRKVA KTYVGRDSIV
EKIVVPHTER KVDTTAAVED ICNEATTQLV HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV
RKRHMQVEII SKKSVRARVK RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR
FKNERVDQSK LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS
MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT QALSPCGKIT
CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA EKLLTRFLQQ KSLVNTNLTA
CVSVKQLIGD RKQAPFTHVL AVSEILFKGN KLTGADLEEA STHMLEIARF LNNRTENMRI
GHLGSFRNKI SSKAHVNNAL MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK
YVIRKHIRGS RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV
TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY MNIFFALLVN
VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL YPDVLRAELP RILVDHDNKT
MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH SGLESEMKTY NVGGMNRDVV TQGAIEMLIK
SIYKPHLMKQ LLEEEPYIIV LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS
ALAQKLTLAD LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL
REGGYAVTSE KVHEMLEKNY VKALKDAWDE LTWLEKFSAI RHSRKLLKFG RKPLIMKNTV
DCGGHIDLSV KSLFKFHLEL LKGTISRAVN GGARKVRVAK NAMTKGVFLK IYSMLPDVYK
FITVSSVLSL LLTFLFQIDC MIRAHREAKV AAQLQKESEW DNIINRTFQY SKLENPIGYR
STAEERLQSE HPEAFEYYKF CIGKEDLVEQ AKQPEIAYFE KIIAFITLVL MAFDAERSDG
VFKILNKFKG ILSSTEREII YTQSLDDYVT TFDDNMTINL ELNMDELHKT SLPGVTFKQW
WNNQISRGNV KPHYRTEGHF MEFTRDTAAS VASEISHSPA RDFLVRGAVG SGKSTGLPYH
LSKRGRVLML EPTRPLTDNM HKQLRSEPFN CFPTLRMRGK STFGSSPITV MTSGFALHHF
ARNIAEVKTY DFVIIDECHV NDASAIAFRN LLFEHEFEGK VLKVSATPPG REVEFTTQFP
VKLKIEEALS FQEFVSLQGT GANADVISCG DNILVYVASY NDVDSLGKLL VQKGYKVSKI
DGRTMKSGGT EIITEGTSVK KHFIVATNII ENGVTIDIDV VVDFGTKVVP VLDVDNRAVQ
YNKTVVSYGE RIQKLGRVGR HKEGVALRIG QTNKTLVEIP EMVATEAAFL CFMYNLPVTT
QSVSTTLLEN ATLLQARTMA QFELSYFYTI NFVRFDGSMH PVIHDKLKRF KLHTCETFLN
KLAIPNKGLS SWLTSGEYKR LGYIAEDAGI RIPFVCKEIP DSLHEEIWHI VVAHKGDSGI
GRLTSVQAAK VVYTLQTDVH SIARTLACIN RRIADEQMKQ SHFEAATGRA FSFTNYSIQS
IFDTLKANYA TKHTKENIAV LQQAKDQLLE FSNLAKDQDV TGIIQDFNHL ETIYLQSDSE
VAKHLKLKSH WNKSQITRDI IIALSVLIGG GWMLATYFKD KFNEPVYFQG KKNQKHKLKM
REARGARGQY EVAAEPEALE HYFGSAYNNK GKRKGTTRGM GAKSRKFINM YGFDPTDFSY
IRFVDPLTGH TIDESTNAPI DLVQHEFGKV RTRMLIDDEI EPQSLSTHTT IHAYLVNSGT
KKVLKVDLTP HSSLRASEKS TAIMGFPERE NELRQTGMAV PVAYDQLPPK NEDLTFEGES
LFKGPRDYNP ISSTICHLTN ESDGHTTSLY GIGFGPFIIT NKHLFRRNNG TLLVQSLHGV
FKVKNTTTLQ QHLIDGRDMI IIRMPKDFPP FPQKLKFREP QREERICLVT TNFQTKSMSS
MVSDTSCTFP SSDGIFWKHW IQTKDGQCGS PLVSTRDGFI VGIHSASNFT NTNNYFTSVP
KNFMELLTNQ EAQQWVSGWR LNADSVLWGG HKVFMSKPEE PFQPVKEATQ LMNELVYSQG
EKRKWVVEAL SGNLRPVAEC PSQLVTKHVV KGKCPLFELY LQLNPEKEAY FKPMMGAYKP
SRLNREAFLK DILKYASEIE IGNVDCDLLE LAISMLVTKL KALGFPTVNY ITDPEEIFSA
LNMKAAMGAL YKGKKKEALS ELTLDEQEAM LKASCLRLYT GKLGIWNGSL KAELRPIEKV
ENNKTRTFTA APIDTLLAGK VCVDDFNNQF YDLNIKAPWT VGMTKFYQGW NELMEALPSG
WVYCDADGSQ FDSSLTPFLI NAVLKVRLAF MEEWDIGEQM LRNLYTEIVY TPILTPDGTI
IKKHKGNNSG QPSTVVDNTL MVIIAMLYTC EKCGINKEEI VYYVNGDDLL IAIHPDKAER
LSRFKESFGE LGLKYEFDCT TRDKTQLWFM SHRALERDGM YIPKLEEERI VSILEWDRSK
EPSHRLEAIC ASMIEAWGYD KLVEEIRNFY AWVLEQAPYS QLAEEGKAPY LAETALKFLY
TSQHGTNSEI EEYLKVLYDY DIPTTENLYF QSGTVDAGAD AGKKKDQKDD KVAEQASKDR
DVNAGTSGTF SVPRINAMAT KLQYPRMRGE VVVNLNHLLG YKPQQIDLSN ARATHEQFAA
WHQAVMTAYG VNEEQMKILL NGFMVWCIEN GTSPNLNGTW VMMDGEDQVS YPLKPMVENA
QPTLRQIMTH FSDLAEAYIE MRNRERPYMP RYGLQRNITD MSLSRYAFDF YELTSKTPVR
AREAHMQMKA AAVRNSGTRL FGLDGNVGTA EEDTERHTAH DVNRNMHTLL GVRQ
