POLG_PVYCH
ID POLG_PVYCH Reviewed; 327 AA.
AC P21294;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 80.
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 Chinese) (PVY).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12218;
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 [GENOMIC RNA].
RX PubMed=2216735; DOI=10.1093/nar/18.18.5554;
RA Zhou X.R., Fang R.X., Wang C.Q., Mang K.Q.;
RT "cDNA sequence of the 3'-coding region of PVY genome (the Chinese
RT isolate).";
RL Nucleic Acids Res. 18:5554-5554(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; X54058; CAA37993.1; -; Genomic_RNA.
DR PIR; S11435; S11435.
DR SMR; P21294; -.
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 3: Inferred from homology;
KW Capsid protein; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW Transferase; Virion.
FT CHAIN <1..60
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040395"
FT CHAIN 1..327
FT /note="Genome polyprotein"
FT /id="PRO_0000420015"
FT CHAIN 61..327
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040396"
FT REGION 65..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 60..61
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 327 AA; 36868 MW; 8F8355E2DE6F2F18 CRC64;
QQQPFATIAQ EGKAPYIASM ALRKLYMDRA VDEEELRAFT EMMVALDDEF EFDSYEVHHQ
ANDTIDAVGD NKKDAKPEQG SIQSNPNKGK EKDVNAGTSG THTVPRIKAI TPKMRMPKSK
GATVLNLEHL LEYAPQQIDI SNTRATQSQF DTWYEAVRMA YDIGETEMPT VMNGLMVWCI
ENGTSPNVNG VWVMMDGNEQ VGYPLKPIVE NAKPTLRQIM AHFSDVAEAY IEMRNKKEPY
MPRYGLIRNL RDVGLARYAF DFYEVTSRTP VRAREAHIQM KAAALKSAQP RLFGLDGGIS
TQEENTERHT TEDVSPSMHT LLGVKNM