ID   POLG_WMV2A              Reviewed;         302 AA.
AC   P20235;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 76.
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 Australia).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=148358;
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=2794980; DOI=10.1099/0022-1317-70-10-2775;
RA   Frenkel M.J., Ward C.W., Shukla D.D.;
RT   "The use of 3' non-coding nucleotide sequences in the taxonomy of
RT   potyviruses: application to watermelon mosaic virus 2 and soybean mosaic
RT   virus-N.";
RL   J. Gen. Virol. 70:2775-2783(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 22-302.
RX   PubMed=2719555; DOI=10.1007/bf01311116;
RA   Yu M.H., Frenkel M.J., McKern N.M., Shukla D.D., Strike P.M., Ward C.W.;
RT   "Coat protein of potyviruses. 6. Amino acid sequences suggest watermelon
RT   mosaic virus 2 and soybean mosaic virus-N are strains of the same
RT   potyvirus.";
RL   Arch. Virol. 105:55-64(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: [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}.
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DR   EMBL; D00535; BAA00423.1; -; Genomic_RNA.
DR   PIR; PS0084; PS0084.
DR   SMR; P20235; -.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001592; Poty_coat.
DR   Pfam; PF00767; Poty_coat; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW   Transferase; Virion.
FT   CHAIN           <1..21
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040493"
FT   CHAIN           1..302
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420032"
FT   CHAIN           22..302
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040494"
FT   REGION          28..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            21..22
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   302 AA;  33860 MW;  D3AF006C844EB234 CRC64;
     KYLEVLDFNH IDGCCESVSL QSGKEAVENL DTGKDSKKDT SGKGDKPQNS QTGQGSKEQT
     KIGTVSKDVN VGSKGKEVPR LQKITKKMNL PTVGGKIILS LDHLLEYKPN QVDLFNTRAT
     KTEFESWYSA VKIEYDLNDE QMGVIMNGFM VWCIDNGTSP DVNGVWVMMD GEEQVEYPLK
     PIVENAKPTL RQIMHHFSDA AEAYIEMRNS ESPYMPRYGL LRNLRDRELA RYAFDFYEVT
     SKTPNRAREA IAQMKAAALA GINSRLFGLD GNISTNSENT ERHTARDVNQ NMHTLLGMGP
     PQ