ID   POLG_WMV2U              Reviewed;        1017 AA.
AC   P18478;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Genome polyprotein;
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   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;
DE   Flags: Fragment;
OS   Watermelon mosaic virus II (isolate USA).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=148360;
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].
RA   Slightom J.L.;
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 736-1016.
RX   PubMed=2374006; DOI=10.1099/0022-1317-71-7-1451;
RA   Quemada H., Sieu L.C., Siemieniak D.R., Gonsalves D., Slightom J.L.;
RT   "Watermelon mosaic virus II and zucchini yellow mosaic virus: cloning of
RT   3'-terminal regions, nucleotide sequences, and phylogenetic comparisons.";
RL   J. Gen. Virol. 71:1451-1460(1990).
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 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=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=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   -!- BIOTECHNOLOGY: The gene for the coat protein is introduced by genetic
CC       manipulation and expressed in squash so as to obtain virus resistant
CC       plants.
CC   -!- MISCELLANEOUS: Readthrough of a terminator codon TGA occurs between
CC       codons for Ala-267 and Gln-269.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; D13913; BAA03009.2; -; Genomic_RNA.
DR   PIR; JQ0498; JQ0498.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; 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:0006508; P:proteolysis; 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; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Genetically modified food; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW   Thiol protease; Transferase; Viral RNA replication; Virion.
FT   CHAIN           <1..219
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040497"
FT   CHAIN           1..1017
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420034"
FT   CHAIN           220..736
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040498"
FT   CHAIN           737..1017
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040499"
FT   DOMAIN          1..195
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          461..585
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          741..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        127
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            219..220
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            736..737
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   1017 AA;  115489 MW;  8853B6411C871E2E CRC64;
     LSVTRKQCLE LGMVLSLSPM GTYLEGTMGC LQLKHGHGGF VIHNTTQLRI HFIQGKDAIL
     IRMPKIFLRL QSATSLDNQN VRNEFAWLEQ TFKRRAYGQQ SQSSSIILPE GKGSFWIHWI
     TTQDGFCGLP LVSVNDGHVV GIHGLTSNDS EKNFFVPFTD GFEKEYLDNA DNLSWDKHWF
     WEPSKIAWGP LNLVEEQPKE EFKISKLVSD LFGNTVAVQS RKERWVLDAM EGNLVACGQA
     DSALVTKHVV KGKCPYFAQY LSLHDGAXQF FEPLMGAYQP SRLNKDAFKK DFFKYNKPVV
     LNEVDFNAFE KAVEGVITMM VDFEFAECLF VTDPDEIYGS LNMKAAVGAQ YKGKKQDYFS
     GMDSFDKERL LYLSCERLFN GEKGIWNGSL KAELRPIEKV QANKTRTFTA APLDTLLGAK
     VCVDDFNNQF YSFNLKCPWT VGMTKFYGGW DKLMRSLPDG WTYCHADGSQ FDSSLTPLLL
     NAVLSIRCCF MEDWWVGREM LENLYAEIVY TPILAPDGTI FKKFRGNNSG QPSTVVDNTL
     MVVIAMYYSC CKQGWSEEDI ERRLVFFANG DDIILAVKDE DVWLYDTLSA SFAELGLNYN
     FDERTKKREE LWFMSHQAML VDGIYIPKLE PERIVSILEW DRSKELMHRT EAICAAMIEA
     WGYTELLQEI RKFYLWLLSK DEFKELAASG KAPYIAETAL RKLYTDVNTQ PSELQRYLEV
     LDFNHIDGCC ESVSLQSGKE TVENLDAGKE SKKDASDKGN KPQNSQVGQG SKEPTKTGTV
     SKDVNVGSKG KEVPRLQKIT KKMNLPTVGG KIILSLDHLL EYKPSQVDLF NTRATKTQFE
     SWYSAVKVEY DLNDEQMGVI MNGFMVWCID NGTSPDVNGV WVMMDGEEQV EYPLKPIVEN
     AKPTLRQIMH HFSDAAEAYI EMRNSESPYM PRYGLLRNLR DRELARYAFD FYEVTSKTPN
     RAREAIAQMK AAALAGVNSR LFGLDGNIST NSENTGRHTA RDVNQNMHTL LGMGPPQ