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}.
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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
//
