ID   POLG_PWVMI              Reviewed;         269 AA.
AC   P32574;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
DE   Flags: Fragment;
OS   Passionfruit woodiness virus (strain Mild) (PWV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31733;
OH   NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH   NCBI_TaxID=185703; Centrosema pubescens.
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
OH   NCBI_TaxID=90550; Macroptilium atropurpureum.
OH   NCBI_TaxID=237841; Passiflora aurantia (Orange-petaled passion flower).
OH   NCBI_TaxID=78168; Passiflora edulis (Passion fruit).
OH   NCBI_TaxID=237871; Passiflora nitida (Bell apple) (Passion flower).
OH   NCBI_TaxID=133504; Passiflora suberosa (Corky-stemmed passion flower).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3202695; DOI=10.1007/bf01310827;
RA   Shukla D.D., McKern N.M., Ward C.W.;
RT   "Coat protein of potyviruses. 5. Symptomatology, serology, and coat protein
RT   sequences of three strains of passionfruit woodiness virus.";
RL   Arch. Virol. 102:221-232(1988).
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: [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   -!- 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   PIR; C60078; VCVSWM.
DR   SMR; P32574; -.
DR   PRIDE; P32574; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   InterPro; IPR001592; Poty_coat.
DR   Pfam; PF00767; Poty_coat; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Virion.
FT   CHAIN           1..269
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040425"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   269 AA;  29934 MW;  B2B4E542267FA919 CRC64;
     KDEIIDAGID GKKGGGKKDT QDAGESNKGK EKDKDINAGS KGSGVPRLQK ITKKMNLPMV
     KGSMVLDLDH LIEYKPDQTK LFNTRATDAQ FATWYEGVKA EYELSDDQMG VIMNPFMVWC
     IENGTSPDIN GVWVMMDGDE QVEYPLKPMV ENAKPTLRQI MHHFSDAAEA YIEMRCASGP
     YMPRYGLLRN LRDKNLARYA FDFYEVNAKT SDRAREAVSG EKAAALSNVT NKLFGLDGNV
     ATISEDTERH TARDVNQNMH TLLGMGAPQ