POLA_CHPVE
ID POLA_CHPVE Reviewed; 622 AA.
AC P10941; P10942; Q04349;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Polyprotein p69;
DE AltName: Full=ORFA polyprotein;
DE Contains:
DE RecName: Full=Papain-like protease p29 {ECO:0000255|PROSITE-ProRule:PRU01225};
DE EC=3.4.22.- {ECO:0000255|PROSITE-ProRule:PRU01225};
DE Contains:
DE RecName: Full=p40 protein;
OS Cryphonectria hypovirus 1 (strain EP713) (CHV-1/EP713) (Chestnut blight
OS fungus hypovirulence-associated virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Duplopiviricetes;
OC Durnavirales; Hypoviridae; Hypovirus.
OX NCBI_TaxID=12478;
OH NCBI_TaxID=5116; Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2721496; DOI=10.1002/j.1460-2075.1989.tb03423.x;
RA Rae B.P., Hillman B.I., Tartaglia J., Nuss D.L.;
RT "Characterization of double-stranded RNA genetic elements associated with
RT biological control of chestnut blight: organization of terminal domains and
RT identification of gene products.";
RL EMBO J. 8:657-663(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2009854; DOI=10.1002/j.1460-2075.1991.tb08004.x;
RA Shapira R., Choi G.H., Nuss D.L.;
RT "Virus-like genetic organization and expression strategy for a double-
RT stranded RNA genetic element associated with biological control of chestnut
RT blight.";
RL EMBO J. 10:731-739(1991).
RN [3]
RP SEQUENCE REVISION, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=1996319; DOI=10.1073/pnas.88.4.1167;
RA Choi G.H., Shapira R., Nuss D.L.;
RT "Cotranslational autoproteolysis involved in gene expression from a double-
RT stranded RNA genetic element associated with hypovirulence of the chestnut
RT blight fungus.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1167-1171(1991).
RN [4]
RP ACTIVE SITES OF PAPAIN-LIKE PROTEASE P29, AND MUTAGENESIS OF CYS-147;
RP CYS-162; CYS-182; HIS-212; HIS-215; GLN-223; LEU-230; GLN-233; ALA-234 AND
RP GLY-248.
RX PubMed=1853573; DOI=10.1016/0042-6822(91)91004-z;
RA Choi G.H., Pawlyk D.M., Nuss D.L.;
RT "The autocatalytic protease p29 encoded by a hypovirulence-associated virus
RT of the chestnut blight fungus resembles the potyvirus-encoded protease HC-
RT Pro.";
RL Virology 183:747-752(1991).
RN [5]
RP CHARACTERIZATION OF PAPAIN-LIKE PROTEASE P29.
RX PubMed=8411354; DOI=10.1128/jvi.67.11.6513-6521.1993;
RA Craven M.G., Pawlyk D.M., Choi G.H., Nuss D.L.;
RT "Papain-like protease p29 as a symptom determinant encoded by a
RT hypovirulence-associated virus of the chestnut blight fungus.";
RL J. Virol. 67:6513-6521(1993).
RN [6]
RP MUTAGENESIS OF CYS-38; CYS-48; CYS-70 AND CYS-72.
RX PubMed=10516056; DOI=10.1128/jvi.73.11.9478-9484.1999;
RA Suzuki N., Chen B., Nuss D.L.;
RT "Mapping of a hypovirus p29 protease symptom determinant domain with
RT sequence similarity to potyvirus HC-Pro protease.";
RL J. Virol. 73:9478-9484(1999).
RN [7]
RP FUNCTION OF P40.
RX PubMed=12097588; DOI=10.1128/jvi.76.15.7747-7759.2002;
RA Suzuki N., Nuss D.L.;
RT "Contribution of protein p40 to hypovirus-mediated modulation of fungal
RT host phenotype and viral RNA accumulation.";
RL J. Virol. 76:7747-7759(2002).
RN [8]
RP FUNCTION OF P29 AND P40 IN DOUBLE-STRANDED RNA REPLICATION, AND MUTAGENESIS
RP OF CYS-70 AND CYS-72.
RX PubMed=14557655; DOI=10.1128/jvi.77.21.11697-11707.2003;
RA Suzuki N., Maruyama K., Moriyama M., Nuss D.L.;
RT "Hypovirus papain-like protease p29 functions in trans to enhance viral
RT double-stranded RNA accumulation and vertical transmission.";
RL J. Virol. 77:11697-11707(2003).
RN [9]
RP FUNCTION.
RX PubMed=16757737; DOI=10.1128/ec.00373-05;
RA Segers G.C., van Wezel R., Zhang X., Hong Y., Nuss D.L.;
RT "Hypovirus papain-like protease p29 suppresses RNA silencing in the natural
RT fungal host and in a heterologous plant system.";
RL Eukaryot. Cell 5:896-904(2006).
CC -!- FUNCTION: P40 protein is involved in reduction of conidiation of the
CC host. Not necessary for replication. Also involved in reduction of
CC orange pigmentation of the host.
CC -!- FUNCTION: [Papain-like protease p29]: Cysteine protease of the
CC peptidase family C7 that contributes to hypovirulence-associated traits
CC like the reduction in conidiation and laccase activity, but not to
CC virulence attenuation. Acts as suppressor of RNA-mediated gene
CC silencing, also known as post-transcriptional gene silencing (PTGS), a
CC mechanism of viral defense that limits the accumulation of viral RNAs.
CC Enhances viral dsRNA accumulation and virus transmission. Also involved
CC in the reduction in orange pigmentation of the host, an effect
CC independent of the intrinsic protease activity. {ECO:0000255|PROSITE-
CC ProRule:PRU01225}.
CC -!- PTM: [Papain-like protease p29]: Autocatalytically processed.
CC {ECO:0000269|PubMed:1996319}.
CC -!- MISCELLANEOUS: Hypoviruses induce hypovirulence in their fungal host
CC Cryphonectria parasitica. The consequence is attenuation of the related
CC fungal disease, chestnut blight, that causes cankers that enlarge and
CC kill branches and trunks. The virus-like genetic elements consist of
CC cytoplasmically replicating double-stranded RNA.
CC -!- MISCELLANEOUS: CHV-1 strain EP713 is a highly hypovirulent strain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA32666.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA32667.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X14524; CAA32666.1; ALT_FRAME; mRNA.
DR EMBL; X14524; CAA32667.1; ALT_FRAME; mRNA.
DR EMBL; M57938; AAA67457.1; -; Genomic_RNA.
DR PIR; S03833; S03833.
DR PIR; S15009; S15009.
DR RefSeq; NP_041090.1; NC_001492.1.
DR MEROPS; C07.001; -.
DR GeneID; 1403615; -.
DR KEGG; vg:1403615; -.
DR Proteomes; UP000007251; Genome.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR002704; Peptidase_C7_dom.
DR Pfam; PF01830; Peptidase_C7; 1.
DR PROSITE; PS51877; HAV_P29_PRO; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Suppressor of RNA silencing;
KW Thiol protease.
FT CHAIN 1..248
FT /note="Papain-like protease p29"
FT /id="PRO_0000038877"
FT CHAIN 249..622
FT /note="p40 protein"
FT /id="PRO_0000038878"
FT DOMAIN 1..248
FT /note="Peptidase C7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01225"
FT REGION 25..73
FT /note="Involved in colony morphology alteration"
FT ACT_SITE 162
FT /note="For papain-like protease p29 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01225"
FT ACT_SITE 215
FT /note="For papain-like protease p29 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01225"
FT SITE 248..249
FT /note="Cleavage; by papain-like protease p29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01225"
FT MUTAGEN 38
FT /note="C->G: No effect on colony morphology."
FT /evidence="ECO:0000269|PubMed:10516056"
FT MUTAGEN 48
FT /note="C->G: No effect on colony morphology."
FT /evidence="ECO:0000269|PubMed:10516056"
FT MUTAGEN 70
FT /note="C->G: Alters colony morphology, with extremely
FT reduced growth. Complete loss of ability to enhance viral
FT dsRNA replication and virus transmission."
FT /evidence="ECO:0000269|PubMed:10516056,
FT ECO:0000269|PubMed:14557655"
FT MUTAGEN 72
FT /note="C->G: Mild alteration of colony morphology. Complete
FT loss of ability to enhance viral dsRNA replication and
FT virus transmission."
FT /evidence="ECO:0000269|PubMed:10516056,
FT ECO:0000269|PubMed:14557655"
FT MUTAGEN 147
FT /note="C->S: Reduces autocatalytic cleavage."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 162
FT /note="C->S: Complete loss of autocatalytic cleavage of
FT p29."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 182
FT /note="C->S: No effect on autocatalytic cleavage of p29."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 212
FT /note="H->S: Reduces autocatalytic cleavage of p29."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 215
FT /note="H->S: Complete loss of autocatalytic cleavage of
FT p29."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 223
FT /note="Q->K: No effect on autocatalytic cleavage of p29."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 230
FT /note="L->P: Reduces autocatalytic cleavage of p29; when
FT associated with K-233."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 233
FT /note="Q->K: No effect on autocatalytic cleavage of p29.
FT Reduces autocatalytic cleavage of p29; when associated with
FT P-230."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 234
FT /note="A->C: No effect on autocatalytic cleavage of p29."
FT /evidence="ECO:0000269|PubMed:1853573"
FT MUTAGEN 248
FT /note="G->R: Complete loss of autocatalytic cleavage of
FT p29."
FT /evidence="ECO:0000269|PubMed:1853573"
SQ SEQUENCE 622 AA; 69688 MW; AFCB274E2197B732 CRC64;
MAQLRKPSQS LVLSESVDPT TVDPFVSVRT EEVVPAGCIT LWEYRDSCGD VPGPLSHGDL
RRLRTPDGVC KCQVHFELPT VLKSGSTGTV PEHPAVLAAF IGRPRRCSLE QRTKELDSRF
LQLVHGGLPA RPSYMIARPP RPVRGLCSSR NGSLAQFGQG YCYLSAIVDS ARWRVARTTG
WCVRVADYLR LLQWVGRRSF GSFQIEKSAV DHVYHVVVDA EYQSEQDGAL FYQAILGLAE
KDPLARIGGR LNPLAAEFAP GSALRVEPVT PQVTRRKGST RMTGRDPTIV SVGKVGMAIT
SIQDALVATE LRNVNFGRRD TEAECRRLWA RYEVNDYFRR HKAELLKFDA RLRSRMAKKP
ASSRARPSDA KIQCIGWRDR HLLPQRLAGL SKQGRSLVWS RFATSNIRRK TPPCVVNPSA
DPVVHNWKDS AALAVKKIAE ARRRQEIRAA AYAERAKARG QTNVVASISE AIETTLRRNK
TRFALDGLHL AASAIVTTRL RSWNQEEIRA GREFRKSTTS WIWRHVPSSI QDALNLTSVR
DKLDPGRAFG YVQAAVAQGM SDFRRAKRAL AIVAKPVIRN IRDPYEHGFV KRDGKLRHSR
DAFNKKLRTK AVAATKVHKI KF
