ID   POLG_BYMV               Reviewed;        3056 AA.
AC   P17765; Q65887; Q6Y1D8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 protease;
DE              EC=3.4.21.-;
DE     AltName: Full=Leader protease P1;
DE     AltName: Full=N-terminal protein;
DE     AltName: Full=P1 proteinase;
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   Bean yellow mosaic virus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus; Potyvirus phaseoluteum.
OX   NCBI_TaxID=12197;
OH   NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH   NCBI_TaxID=4627; Canna.
OH   NCBI_TaxID=3828; Crotalaria.
OH   NCBI_TaxID=52517; Eustoma.
OH   NCBI_TaxID=58987; Freesia.
OH   NCBI_TaxID=49747; Gladiolus.
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3873; Lupinus luteus (European yellow lupine).
OH   NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH   NCBI_TaxID=3469; Papaver somniferum (Opium poppy).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea) (Lathyrus oleraceus).
OH   NCBI_TaxID=35938; Robinia pseudoacacia (Black locust).
OH   NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
OH   NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
OH   NCBI_TaxID=57577; Trifolium pratense (Red clover).
OH   NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
OH   NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
OH   NCBI_TaxID=97047; Trifolium vesiculosum.
OH   NCBI_TaxID=78534; Trigonella foenum-graecum (Fenugreek).
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
OH   NCBI_TaxID=3908; Vicia sativa (Spring vetch) (Tare).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate GDD;
RX   PubMed=14648299; DOI=10.1007/s00705-003-0185-7;
RA   Hammond J., Hammond R.W.;
RT   "The complete nucleotide sequence of isolate BYMV-GDD of Bean yellow mosaic
RT   virus, and comparison to other potyviruses.";
RL   Arch. Virol. 148:2461-2470(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2775-3056.
RX   PubMed=2671258; DOI=10.1099/0022-1317-70-8-1961;
RA   Hammond J., Hammond R.W.;
RT   "Molecular cloning, sequencing and expression in Escherichia coli of the
RT   bean yellow mosaic virus Capsid protein gene.";
RL   J. Gen. Virol. 70:1961-1974(1989).
RN   [3]
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: [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 (By
CC       similarity). Reduces the abundance of host transcripts related to
CC       jasmonic acid biosynthesis therefore altering the host defenses (By
CC       similarity). In order to increase its own stability, decreases host
CC       protein degradation pathways (By similarity).
CC       {ECO:0000250|UniProtKB:P13529, ECO:0000250|UniProtKB:P89509}.
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 (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: [Nuclear inclusion protein B]:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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: [Nuclear inclusion protein A]:
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: [Helper component proteinase]:
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 (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: [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=P17765-1; Sequence=Displayed;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ95-1; 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   -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC       translation.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY192568; AAP30002.1; -; Genomic_RNA.
DR   EMBL; D00490; BAA00378.1; -; Genomic_RNA.
DR   PIR; JU0115; JU0115.
DR   MEROPS; C04.008; -.
DR   MEROPS; C06.001; -.
DR   MEROPS; S30.002; -.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0044161; C:host cell cytoplasmic vesicle; 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 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:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
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-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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   3: Inferred from homology;
KW   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; Ribosomal frameshifting;
KW   RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW   Thiol protease; Transferase; Viral immunoevasion; Viral RNA replication;
KW   Virion.
FT   CHAIN           1..3056
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000419996"
FT   CHAIN           1..284
FT                   /note="P1 protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040256"
FT   CHAIN           285..741
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040257"
FT   CHAIN           742..1089
FT                   /note="Protein P3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040258"
FT   CHAIN           1090..1142
FT                   /note="6 kDa protein 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040259"
FT   CHAIN           1143..1777
FT                   /note="Cytoplasmic inclusion protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040260"
FT   CHAIN           1778..1830
FT                   /note="6 kDa protein 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040261"
FT   CHAIN           1831..2021
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040262"
FT   CHAIN           2022..2264
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040263"
FT   CHAIN           2265..2783
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040264"
FT   CHAIN           2784..3056
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040265"
FT   DOMAIN          139..284
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          619..741
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1214..1366
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1385..1544
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2022..2240
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2507..2630
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          2788..2820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           335..338
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           593..595
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1316..1319
FT                   /note="DECH box"
FT   MOTIF           1871..1878
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2792..2811
FT                   /note="Basic and acidic 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        232
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        627
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        700
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2067
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2102
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2172
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   BINDING         1227..1234
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            741..742
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1089..1090
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            1100..1101
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1142..1143
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            1152..1153
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1777..1778
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            1787..1788
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1830..1831
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            1840..1841
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2021..2022
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2265..2266
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2274..2275
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2783..2784
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250|UniProtKB:P18247"
FT   SITE            2793..2794
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1893
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09814"
FT   MOD_RES         3040
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P17767"
FT   VARIANT         2775
FT                   /note="D -> G"
FT   VARIANT         2805
FT                   /note="D -> N"
FT   VARIANT         2855
FT                   /note="L -> F"
FT   VARIANT         2862
FT                   /note="E -> K"
FT   VARIANT         2897
FT                   /note="Q -> R"
FT   VARIANT         2975
FT                   /note="G -> E"
FT   VARIANT         2994
FT                   /note="K -> E"
FT   VARIANT         3017
FT                   /note="G -> A"
SQ   SEQUENCE   3056 AA;  347722 MW;  BA4D2F2D2D4624B3 CRC64;
     MTTINIGTIP VVINQNADTQ MGEGTKNIFP IVKDFVDPFA DLEMRCAERV KRMGELCFSK
     KGRYITMIPK PDYIKAREKE QREEELNFQN SEHVLNSLDT TCTPEHHSSR NNGMQVSFKT
     QHYKRTFRKP RIQAKKRDLK GQHTIHYVAK ELLSIVKKRD MVLEVVDKRK HANFATFRRY
     GKTYGMHITL NHMVRKRRRV DVTLNKLMTE IAMHCAIPFE CLNTLTLRKG HSGLVLQTET
     VPNVHKIKSK ITIVRGVVNE GNIPVLIDAR KKLSGRDMST IREFSAGDLF WKGYNQTFID
     NRPTDLNHQC TSDLNVTQCG SVMALLTLAL FPCGRITCKK CVENFLNQNN KERFNNASVF
     INQVIQLLEK GFSEFKHSKE ILLMFKERLQ MENPATDQCM EIAKATAALP EAPFSHIKEI
     NNVLLKYGSL SNEEVGGASK HLLEVVRYIR NRTDSIQRND LSKFRNKISS KTHINLDLMC
     DNQLDKNANF VWGQRAYHAK RFLSNYFNEI NPSEGYDKFI FRKLPNGARE LAIGRLIMPT
     NFEAFREQMK GKMIDNGPIG KDCVSRMRGS FCYPCCCTTD DVGTAVISDF KMPTKYHLVL
     GGNDLAKYIK LPTDTTGNMY IAKDGFCHIN IFFAMLVNVS EEKSKDFTKM VRDQIMPKLG
     EWPTMMDVAT ACWQLTVWFP DTLSAELPRI LVDHKLGIMH VLDSYGSISA GYHVLKANIV
     SQLIKFASDD LESELKYYRV GGDCNFGSRV RIDTKFLLKS IYRPDLLERI IEHEPFVLVL
     AMQSPAVLLA LFNSASLEKA VQYWMHREMQ VSHIMTLLAV LASNVSASKL LTTQFEIIEA
     SAPQILAEMD KVHLPMHSIH SANVFLMNMS ESRETDKTID ELGFYSFKKS SRILMEKTLM
     ADLEEQWQGL GLLERLSLIK RSWRVRAKYS SFAIQREEPG IRDKFTTSLK LSGAQIKQQL
     LAQKDQAVHF VERRIEGTKK FVANQSISLI KMCLPRLADI VNILTVIALL NAILAFMLDH
     IKRFNEARRI AQEKKEKQHL KELNTLYNKY WDNEKPTYLE FKSDVIEKLP HTLATFEKYY
     FEDDKYTFQA KPNDMVALEK IIAVTALVLM IFDAERSDCV YKVLNKLKGI LSTTTQDAYR
     FQSLDTSKTL LEEKEMTIDF EINEGEVKAF SGTQTTFSEW WDNQLQNGNV ITHYRTEGQF
     MEFTRANAQP VANEIAHNDA HDILVRGAVG SGKSTGLPFY LSNKGKVLMI ESTRPLAENV
     FKQLKSEPFY ASPTLRMRGT TSYGASPITI MTSGYALHYY ANNPAMMKEY KFVIIDECHV
     HDANAIAFVS LLKEYSFDGK LIKVSATPPG REVEFTTQYP VTLVTEESLS FEQFVSQQGT
     GANCDMLDVC DNILVYVASY NEVDQLSKML LDRGHIVTKV DGRTMKNGKT EIESKGSRSK
     RHFIVATNII ENGVTLDIEG VVDFGLKVVP ELDVDNRLMR YTKQNVSYGE RIQRLGRVGR
     HKAGKALRIG VTEKGLVKPP SVITTEAAFY CFAYGLPVMA EGVTPSLLSK CTVQQARSMM
     SFELPIMYTV NLVRFDGTMH PSVHNLLKPY KLRDSNVVLN KMAIPHGNVR NWPTVRDFKC
     MGVRIDAPED TRVPFHARDI PDKLHKEIFE VCCKYKGDAG FSKLNVVNAC KIAYTLQTDP
     SSIQRTIKIL DELIAREQQK REYFQNVANT SCAGSSYSLS NIINAIRARS TSDYTQENLS
     VLHSARAQLL EFKNINSDFS NLSTLSEFGA LECLQFESLQ EISKHLQLKG HWNKPVLIQD
     FLIAAGVLGG GCWMLYQYFK QETSKAFVFQ GKNRRTKQKL RFRDARDMKG RMEVYADEGT
     IVENFGSKYT KKGKVRGTTT GMGTKTRRFT NMYGFDPTEY SFARYLDPIT GETLDEQPIT
     NLNLVSEHFQ EMRRKYRENE IMESQQFAAN PRIEAYFVKD AGQKVLKVDL TPHKPLLYSD
     KFGNIMGYPE REGELRQTGA AEFIDPKELP EPKESTDFDF ESLSKIGGLR DYNPIAANVC
     LLENESAEYC DEIYGIGYGN VIITNQHLFR HNNGELTIKS KHGTFKCKNT CALKLLPIEG
     HDLLLIQMPK DFPVFPQKLR FREPTHEDKI VLVSTNFQEK SFSSVVSESS NISRVKQANF
     FKHWISTVAG QCGNPMVSTK DGFIVGIHSL TAVSGDLNVF TSIPPNFEDE VLKQMSKKSW
     CCGWKLNMSQ IGWDGIKIVD DQPKDPFPVS KMVGLLNDLQ LSFQSAKNTK WLLERAHGNI
     KAVAQASSAL VTKHVVKGKC RLFEVYLTTD EEAEKFFRPL MGAYQKSRLN KEAYVKDLMK
     YATPIEVGLV DTRCFERSFE KVQNMLELKG FSKCNYVTYG PDILSALNMK AAMGALYSGK
     KKDHFSEISE EKFDNILQAS CERLYSGRMG VWNGSLKAEL RPQEKVLANK TRSFTAAPID
     TLLAGKVCVD DFNNKFYSLH LKIPSTVGIT KFYGGWDRLL DSLPDGWVYC DADGSQFDSS
     LTPYLLNAVL EMRLRLMEEW DLGEQMLKNL YTEIVYTPIL TPDGTIVKKF KGNNSGQPST
     VVDNTLMVIM AVYYAAEKLG IKGNLEDTLV FFANGDDLLI AIKPECESYL DKFEGLFSEL
     GLKYDFSSRT KNKGDLWFMS HRGIQIDGMW IPKLEEERIV SILEWDRAIQ PEHRLEAICA
     AMIEAWGYPT LLNHIRKFYL WVLGQAPYSQ LSAEGKAPYI SEVALKHLYT EEKVTPTELE
     RYNIALIDCF ESESDEVLTC RFQSDQEQLN AGEEKKDKRK KNEGDPNKDS EGQSVRQIVP
     DRDVNAGTVG TFSVPRLKKI AGKLNIPKIG GKIVLNLDHL LEYNPPQDDI SNVIATQAQF
     EAWYNGVKQA YEVEDSQMGI ILNGLMVWCI ENGTSGDLQG EWTMMDGEEQ VTYPLKPILD
     NAKPTFRQIM SHFSEVAEAY IEKRNATERY MPRYGLQRNL TDYGLARYAF DFYKLTSRTP
     VRAREAHMQM KAAAVRGKST RLFGLDGNVG TDEENTERHT AGDVNRDMHT MLGVRI
//