ID   POLG_WMV2T              Reviewed;         455 AA.
AC   Q89251;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 3.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-B;
DE              Short=NIB;
DE     AltName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
DE   Flags: Fragment;
OS   Watermelon mosaic virus II (isolate Tonga) (Vanilla necrosis potyvirus)
OS   (VNV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=148359;
OH   NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH   NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8470960; DOI=10.1007/bf01316887;
RA   Wang Y.Y., Beck D.L., Gardner R.C., Pearson M.N.;
RT   "Nucleotide sequence, serology and symtomology suggest that vanilla
RT   necrosis potyvirus is a strain of watermelon mosaic virus II.";
RL   Arch. Virol. 129:93-103(1993).
RN   [2]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
CC   -!- FUNCTION: [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   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC   -!- PTM: Genome polyprotein of potyviruses undergoes post-translational
CC       proteolytic processing by the main proteinase NIa-pro resulting in the
CC       production of at least ten individual proteins. The P1 proteinase and
CC       the HC-pro cleave only their respective C-termini autocatalytically.
CC       6K1 is essential for proper proteolytic separation of P3 from CI (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA48497.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L22907; AAA48497.2; ALT_INIT; Genomic_RNA.
DR   SMR; Q89251; -.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN           <1..174
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040495"
FT   CHAIN           1..455
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420033"
FT   CHAIN           175..455
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040496"
FT   REGION          182..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        5
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000250"
FT   SITE            174..175
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   455 AA;  51607 MW;  937AFDEAE9A52EC1 CRC64;
     RTGSCANGDD IILAVKGEDV WLYDTLSASF AELGLNYNFD ERTKKREELW FMSHQAMLVD
     GIYIPKLEPE RIVSILEWDR SKELMHRTEA ICAAMIEAWG YTELLQEIRK FYLWLLSKDE
     FKELAASGKA PYIAETALRK LYTNVNTQPN ELQRYLEVLD FNHIDGCCES VSLQSGKETV
     ENLDAGKESK KETSDKGNKP QNSQVGQGSK EPTKTGTVSK DVNVGSKGKE VPRLQKITKK
     MNLPTVGGKI ILGLDHLLEY KPNQVDLFNT RATKTQFESW YSAVKVEYDL NDEQMGVIMN
     GFMVWCIDNG TSPDVNGVWV MMDGEEQVEY PLKPIVENAK PTLRQIMHHF SDAAEAYIEM
     RNSESPYMPR YGLLRNLRDR ELARYAFDFY EVTSKTPNRA REAIAQMKAA ALAGINSRLF
     GLDGNISTNS ENTERHTARD VNQNMHTLLG MGPPQ