ID   POLG_PRSVP              Reviewed;         675 AA.
AC   P19723;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 88.
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 P / mutant HA 5-1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31730;
OH   NCBI_TaxID=3649; Carica papaya (Papaya).
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; D00595; BAA00471.1; -; Genomic_RNA.
DR   PIR; JQ0496; JQ0496.
DR   SMR; P19723; -.
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_0000040371"
FT   CHAIN           1..675
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420011"
FT   CHAIN           389..675
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040372"
FT   DOMAIN          92..216
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          397..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..426
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;  77925 MW;  EF3A2B804A05F154 CRC64;
     LVRKRCERLY EGRMGVWNGS LKAELRPAEI VLAKKTRSFT AAPLDTLLGA KVCVDDFNNW
     FYSKNMECPW TVGMTKFYKG WDEFLRKFPD GWVYCDADGS QFDSSLTPYL LNAVLSIRLW
     AMEDWDIGEQ MLKNLYGEIT YTPILTPDGT IVKKFKGNNS GQPSTVVDNT LMVLITMYYA
     LRKAGYDTKT QEDMCVFYIN GDDLCIAIHP DHEHVLDSFS SSFAELGLKY DFAQRHRNKQ
     NLWFMSHRGI LIDDIYIPKL EPERIVAILE WDKSKLPEHR LEAITAAMIE SWGHGDLTHQ
     IRRFYQWVLE QAPFNELAKQ GRAPYVSEVG LRRLYTSERG SMDELEAYID KYFERERGDS
     PELLVYHESR STDDYQLVCS NNTHVFHQSK NEAVDAGLNE KLKEKENQKE KEKEKQKEKE
     KDGASDGNDV STSTKTGERD RDVNVGTSGT FTVPRIKSFT DKMVLPRIKG KTVLNLNHLL
     QYNPQQIDIS NTRATHSQFE KWYEGVRNDY GLNDNEMQVM LNGLMVWCIE NGTSPDISGV
     WVMMDGETQV DYPIKPLIEH ATPSFRQIMA HFSNAAEAYI AKRNATERYM PRYGIKRNLT
     DISLARYAFD FYEVNSKTPD RAREAHMQMK AAALRNTSRK MFGMDGSVSN KEENTERHTV
     EDVNRDMHSL LGMRN