ID   POLG_PRSVW              Reviewed;         675 AA.
AC   P19724;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Papaya ringspot virus (strain W).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12207;
OH   NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH   NCBI_TaxID=3673; Momordica charantia (Bitter gourd) (Balsam pear).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2303800; DOI=10.1099/0022-1317-71-1-203;
RA   Quemada H., L'Hostis B., Gonsalves D., Reardon I.M., Heinrikson R.,
RA   Hiebert E.L., Sieu L.C., Slightom J.L.;
RT   "The nucleotide sequences of the 3'-terminal regions of papaya ringspot
RT   virus strains W and P.";
RL   J. Gen. Virol. 71:203-210(1990).
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}.
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DR   EMBL; D00594; BAA00470.1; -; Genomic_RNA.
DR   PIR; JQ0497; JQ0497.
DR   SMR; P19724; -.
DR   ABCD; P19724; 2 sequenced antibodies.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019028; C:viral capsid; 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Nucleotide-binding; Nucleotidyltransferase;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           <1..388
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040373"
FT   CHAIN           1..675
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420012"
FT   CHAIN           389..675
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040374"
FT   DOMAIN          92..216
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          390..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            388..389
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   675 AA;  78151 MW;  9255D9B51871E824 CRC64;
     LVRKSCERLY EGRMGVWNGS LKAELRPAEK VLAKKTRSFT AAPLDTLLGA KVCVDDFNNW
     FYSKNMECPW TVGMTKFYKG WDEFLRKFPD GWVYCDADGS QFDSSLTPYL LNAVLSIRLW
     AMEDWDIGEQ MLKNLYGEIT YTPILTPDGT IVKKFKGNNS GQPSTVVDNT LMVLITMYYA
     LRKAGYDTKT QEDMCVFYIN GDDLCIAIHP DHEHVLDSFS RSFAELGLKY DFTQRHRNKQ
     NLWFMSHRGI LIDDIYIPKL EPERIVAILE WDKSKLPEHR LEAITAAMIE SWGYGDLTHQ
     IRRFYQWVLE QAPFNELAKQ GRAPYVSEVG LRRLYTSERG SMDELEAYID KYFERERGDS
     PELLVYHESR STDDYQLVCS NNTHVFHQSK NEAVDTGLNE KFKEKEKQKE KEKEKQKEKE
     KDDASDGNDV STSTKTGERD RDVNVGTSGT FTVPRIKSFT DKMILPRIKG KSVLNLNHLL
     QYNPQQIDIS NTRATQSQFE KWYEGVRNDY GLNDNEMQVM LNGLMVWCIE NGTSPDISGV
     WVMMDGETQV DYPIKPLIEH ATPSFRQIMA HFSNAAEAYI AKRNATERYM PRYGIKRNLT
     DISLARYAFD FYEVNSKTPD RAREAHMQMK AAALRNTSRR MFGMDGSVSN KEENTERHTV
     EDVNRDMHSL LGMRN