POLG_PVYYO
ID POLG_PVYYO Reviewed; 284 AA.
AC P11897;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Potato virus Y (strain Yo) (PVY).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12221;
OH NCBI_TaxID=4071; Capsicum (peppers).
OH NCBI_TaxID=4085; Nicotiana.
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2740238; DOI=10.1093/nar/17.11.4401;
RA Bravo-Almonacid F.F., Mentaberry A.N.;
RT "Nucleotide cDNA sequence coding for the PVYo coat protein.";
RL Nucleic Acids Res. 17:4401-4401(1989).
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; X14136; CAA32356.1; -; mRNA.
DR PIR; S04723; S04723.
DR SMR; P11897; -.
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; IPR001592; Poty_coat.
DR Pfam; PF00767; Poty_coat; 1.
PE 2: Evidence at transcript level;
KW Capsid protein; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW Transferase; Virion.
FT CHAIN <1..17
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040423"
FT CHAIN 1..284
FT /note="Genome polyprotein"
FT /id="PRO_0000420020"
FT CHAIN 18..284
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040424"
FT REGION 16..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 17..18
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 284 AA; 31971 MW; E98535C4607898E2 CRC64;
VALDDEFEFD SYEVHHQAND TIDAGGNNKK DAKPEQSSIQ SNLSKGKDKD VNVGTSGTHT
VPRIKAITSK MRMPRSKGVA ALNLEHLLEY APQQIDISNT RATQSQFDTW YEAVRMAYDI
GQTEMPTVMN GLMVWCIENG TSPNINGVWV MMDGNEQVEY PLKPIVENAK PTLRQIMAHF
SDVAEAYIEM RNKKEPYMPR YGLIRNLRDI SLARYAFDFY EVTSRTPVRA REAHIQMKAA
ALKSAQPRLF GLDGGISTQE ENTERHTTED VSPSMHTLLG GKNM