POLG_PVYC
ID POLG_PVYC Reviewed; 856 AA.
AC P22601;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE AltName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Helper component proteinase;
DE Short=HC-pro;
DE EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
DE Contains:
DE RecName: Full=Protein P3;
DE Flags: Fragment;
OS Potato virus Y (strain C) (PVY) (Potato virus C).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12217;
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=2219708; DOI=10.1016/0042-6822(90)90356-v;
RA Thornbury D.W., Patterson C.A., Dessens J.T., Pirone T.P.;
RT "Comparative sequence of the helper component (HC) region of potato virus Y
RT and a HC-defective strain, potato virus C.";
RL Virology 178:573-578(1990).
RN [2]
RP FUNCTION (HELPER COMPONENT PROTEINASE).
RX PubMed=9880030; DOI=10.1099/0022-1317-79-12-3119;
RA Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C., Baker J.,
RA Pirone T.P.;
RT "Mutations in the potyvirus helper component protein: effects on
RT interactions with virions and aphid stylets.";
RL J. Gen. Virol. 79:3119-3122(1998).
RN [3]
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: [Helper component proteinase]: Required for aphid
CC transmission and also has proteolytic activity (By similarity). Only
CC cleaves a Gly-Gly dipeptide at its own C-terminus (By similarity).
CC Interacts with virions and aphid stylets (PubMed:9880030). Acts as a
CC suppressor of RNA-mediated gene silencing, also known as post-
CC transcriptional gene silencing (PTGS), a mechanism of plant viral
CC defense that limits the accumulation of viral RNAs. May have RNA-
CC binding activity (By similarity). {ECO:0000250|UniProtKB:P04517,
CC ECO:0000269|PubMed:9880030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC potyviral polyprotein.; EC=3.4.22.45;
CC Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- DOMAIN: [Helper component proteinase]: The N-terminus is involved in
CC interaction with stylets. The central part is involved in interaction
CC with virions and the C-terminus is involved in cell-to cell movement of
CC the virus.
CC -!- PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes
CC post-translational proteolytic processing by the main proteinase NIa-
CC pro resulting in the production of at least ten individual proteins.
CC The P1 proteinase and the HC-pro cleave only their respective C-termini
CC autocatalytically. 6K1 is essential for proper proteolytic separation
CC of P3 from CI (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M38377; AAA47183.1; -; Genomic_RNA.
DR SMR; P22601; -.
DR PRIDE; P22601; -.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR001456; HC-pro.
DR InterPro; IPR031159; HC_PRO_CPD_dom.
DR InterPro; IPR042308; HC_PRO_CPD_sf.
DR InterPro; IPR002540; Pept_S30_P1_potyvir.
DR InterPro; IPR039560; Potyvirid-P3.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF01577; Peptidase_S30; 1.
DR Pfam; PF13608; Potyvirid-P3; 1.
DR PROSITE; PS51744; HC_PRO_CPD; 1.
DR PROSITE; PS51871; PV_P1_PRO; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Serine protease; Suppressor of RNA silencing;
KW Thiol protease.
FT CHAIN 1..856
FT /note="Genome polyprotein"
FT /id="PRO_0000420018"
FT CHAIN 1..284
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040417"
FT CHAIN 285..740
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040418"
FT CHAIN 741..>856
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040419"
FT DOMAIN 141..284
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 618..740
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 592..594
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 192
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 201
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 235
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 626
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 699
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 284..285
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 740..741
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT NON_TER 856
SQ SEQUENCE 856 AA; 96829 MW; 959EAE29BA0D60A8 CRC64;
MAIYMSTICF GSIECKLPYS PASCGHVTEE REVLASVEPF MDLEAQLSAR LLRQKHATVR
VLKNGTCAYR YKTDAQIVRI QKKLERKERD EYHFQMAAPS IVSKITIAGG DPPSKYEPQT
PKRVIHTTPR VRKVKKHSII KLTESQMNHL IKQVKRIMSA KKGSVHLINK KSTHVQYKEI
LGTTRAAVRT AHMMGLRRRV DFRCDMWTTE RLKCLARTDK WSNRVHTINI RKGDSGVILN
ADSLKGHFGR SSGGLFIVRG SHEGKLYDAR SKVTQGVLNS MVQFSNAENF WKGLDDNWAR
MRYPSDHTCI DGLPVEDCGR VAALMTHSIL PCYEITCPTC AQQYANLPAS DLFKLLHKHA
RDGLSRLGSD KDRFVHVNKF LVALEHLTEP VDLNLELFNE IFKSIGEKQQ APFKNLNVLN
NFFLKGKENT AHEWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
NQLDKNANFL WGQREYHAKR FFSNFFEEVD PAKGYSAYEI RKHPNGTRKL SIGNLVVPLD
LAEFRQKMKG DYRKQPGVSK RCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG
NSGDQKYVDL PKGDSEMLYI AKQGYCYINV FLAMLINVSE EDAKDFTKKV RDMCVPKLGT
WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV VDSFGSQTTG YHILKASSVS
QLILFANDEL ESEIKHYRVG GVPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPK
VMRQLLLDEP HLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
SAAETLVAQR IIIDAA
