POLG_PVYO
ID POLG_PVYO Reviewed; 856 AA.
AC P22602;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 O) (PVY).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12220;
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 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. Only cleaves a Gly-Gly
CC dipeptide at its own C-terminus. Interacts with virions and aphid
CC stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC known as post-transcriptional gene silencing (PTGS), a mechanism of
CC plant viral defense that limits the accumulation of viral RNAs. May
CC have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M37180; AAA47184.1; -; Genomic_RNA.
DR PIR; A46341; A46341.
DR SMR; P22602; -.
DR ABCD; P22602; 3 sequenced antibodies.
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; Thiol protease.
FT CHAIN 1..856
FT /note="Genome polyprotein"
FT /id="PRO_0000420019"
FT CHAIN 1..284
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040420"
FT CHAIN 285..740
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040421"
FT CHAIN 741..>856
FT /note="Protein P3"
FT /id="PRO_0000040422"
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 334..337
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
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; 96813 MW; 4645EB6D5FD0A0A2 CRC64;
MATYMSTICF GSFECKLPYS PASCGHIVKE REVPASVDPF ADLETQLSAR LRKQEYATVR
VLKNGTFTYR YKTDAQIMRI QKKLERKDRE EYHFQMAAPS IVSKITIAGG DPPSKSEPQA
PRGIIHTTPK VRKVKTRPII KLTEGQMNHL IKQVKQIMSE KRGSVHLISK KTTHVQYKEI
LGATRAAVRT AHMMGLRRRV DFRCDTWTVG LLQRLARTDK WSNQVRTIHV RRGDSGVILN
TKSLKGHFGR SSGDLFIVRG SHEGKLYDAR SRVTQSVLNS MIQFSNADNF WKGLDGNWAR
MRYPSDHTCV AGLPVADCGR VAALTRHSIL PCYKITCPTC AQQYASLPVS DLFKLLHKHA
RDGLNRLGAD KDRFIHVNKF LMALEHLTEP VDLNLELFNE IFKSIGEKQQ APFKNLNVLN
NFFLKGKENT AHEWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAR ANWNLYLSCD
NQLDKNANFL WGQREYHAKR FFSNFFDEID PAKGYSAYEI RKHPNGTRKL SIGNLVVPLD
LAEFRQKMKG DYRKQPGVSR KCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG
NSGDQKFVDL PKGDSEMLYI AKQGYCYINV FLAMLINISE EDAKDFTKKV RDMCVPKLGT
WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV VDSFGSQTTG YHILKASSVS
QLILFANDEL ESDIKHYRVG GVPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPR
VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
SAAETLVAQR IIIDAA
