ID   POLG_PEMV               Reviewed;         381 AA.
AC   P07993;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 74.
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   Pepper mottle virus (PeMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12209;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=4075; Datura inoxia (Downy thornapple) (Datura meteloides).
OH   NCBI_TaxID=4107; Solanum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Dougherty W.G., Allison R.F., Parks T.D., Johnston R.E., Feild M.J.,
RA   Armstrong F.B.;
RT   "Nucleotide sequence at the 3' terminus of pepper mottle virus genomic RNA:
RT   evidence for an alternative mode of potyvirus capsid protein gene
RT   organization.";
RL   Virology 146:282-291(1985).
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=AAA46902.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M11598; AAA46902.1; ALT_FRAME; Genomic_RNA.
DR   PIR; A26205; A26205.
DR   SMR; P07993; -.
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; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001592; Poty_coat.
DR   Pfam; PF00767; Poty_coat; 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..114
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227541"
FT   CHAIN           1..381
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420038"
FT   CHAIN           115..381
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000219918"
FT   REGION          115..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            114..115
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   381 AA;  43220 MW;  1F942BD7B44364A3 CRC64;
     YVPKLEEERI VIYSTMDRAD LAEHRLEAIC AAMIESWGYS ELTHQIRRFY SWLLQQQPFA
     SIAQEGKAPY IASMALRKLY MDRAVDEEEL RVFTEMMVAL DDEFECDSYE VHHQANDTID
     TGGNSKKDVK PEQGSIQPSS NKGKEKDVNA GTSGTHTVPR IKAITAKMRM PKSKGAAVLK
     LDHLLEYAPQ QIDISNTRAT QSQFDTWYEA VRVAYDIGET EMPTVMNGLM VWCIENGTSP
     NINGVWVMMD GSEQVEYPLK PIVENAKPTL RQIMAHFSDV AEAYIEMRNK KEPYMPRYGL
     VRNLRDASLA RYAFDFYEVT SRTPVRAREA HIQMKAAALK SAQSRLFGLD GGVSTQEENT
     ERHTTEDVSP SMHTLLGVKN M