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Protein

Polyprotein p69

Gene
N/A
Organism
Cryphonectria hypovirus 1 (strain EP713) (CHV-1/EP713) (Chestnut blight fungus hypovirulence-associated virus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Papain-like protease p29 is a cysteine protease that contributes to hypovirulence-associated traits like the reduction in conidiation and laccase activity, but not to virulence attenuation. Acts as suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of viral defense that limits the accumulation of viral RNAs. Enhances viral dsRNA accumulation and virus transmission. Also involved in the reduction in orange pigmentation of the host, an effect independent of the intrinsic protease activity.
P40 protein is involved in reduction of conidiation of the host. Not necessary for replication. Also involved in reduction of orange pigmentation of the host.

Miscellaneous

Hypoviruses induce hypovirulence in their fungal host Cryphonectria parasitica. The consequence is attenuation of the related fungal disease, chestnut blight, that causes cankers that enlarge and kill branches and trunks. The virus-like genetic elements consist of cytoplasmically replicating double-stranded RNA.
CHV-1 strain EP713 is a highly hypovirulent strain.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei162For papain-like protease p29 activitySequence analysis1
Active sitei215For papain-like protease p29 activitySequence analysis1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease, Suppressor of RNA silencing, Thiol protease

Protein family/group databases

MEROPSiC07.001

Names & Taxonomyi

Protein namesi
Recommended name:
Polyprotein p69
Alternative name(s):
ORFA polyprotein
Cleaved into the following 2 chains:
OrganismiCryphonectria hypovirus 1 (strain EP713) (CHV-1/EP713) (Chestnut blight fungus hypovirulence-associated virus)
Taxonomic identifieri12478 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesHypoviridaeHypovirus
Virus hostiCryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica) [TaxID: 5116]
Proteomesi
  • UP000007251 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38C → G: No effect on colony morphology. 1 Publication1
Mutagenesisi48C → G: No effect on colony morphology. 1 Publication1
Mutagenesisi70C → G: Alters colony morphology, with extremely reduced growth. Complete loss of ability to enhance viral dsRNA replication and virus transmission. 2 Publications1
Mutagenesisi72C → G: Mild alteration of colony morphology. Complete loss of ability to enhance viral dsRNA replication and virus transmission. 2 Publications1
Mutagenesisi147C → S: Reduces autocatalytic cleavage. 1 Publication1
Mutagenesisi162C → S: Complete loss of autocatalytic cleavage of p29. 1 Publication1
Mutagenesisi182C → S: No effect on autocatalytic cleavage of p29. 1 Publication1
Mutagenesisi212H → S: Reduces autocatalytic cleavage of p29. 1 Publication1
Mutagenesisi215H → S: Complete loss of autocatalytic cleavage of p29. 1 Publication1
Mutagenesisi223Q → K: No effect on autocatalytic cleavage of p29. 1 Publication1
Mutagenesisi230L → P: Reduces autocatalytic cleavage of p29; when associated with K-233. 1 Publication1
Mutagenesisi233Q → K: No effect on autocatalytic cleavage of p29. Reduces autocatalytic cleavage of p29; when associated with P-230. 1 Publication1
Mutagenesisi234A → C: No effect on autocatalytic cleavage of p29. 1 Publication1
Mutagenesisi248G → R: Complete loss of autocatalytic cleavage of p29. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000388771 – 248Papain-like protease p29Add BLAST248
ChainiPRO_0000038878249 – 622p40 proteinAdd BLAST374

Post-translational modificationi

Papain-like protease p29 is autocatalytically processed.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei248 – 249Cleavage; by papain-like protease p292

Proteomic databases

PRIDEiP10941

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 243Peptidase C7Sequence analysisAdd BLAST243

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 73Involved in colony morphology alterationAdd BLAST49

Phylogenomic databases

OrthoDBiVOG090002CP

Family and domain databases

InterProiView protein in InterPro
IPR002704 Peptidase_C7_dom
PfamiView protein in Pfam
PF01830 Peptidase_C7, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10941-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQLRKPSQS LVLSESVDPT TVDPFVSVRT EEVVPAGCIT LWEYRDSCGD
60 70 80 90 100
VPGPLSHGDL RRLRTPDGVC KCQVHFELPT VLKSGSTGTV PEHPAVLAAF
110 120 130 140 150
IGRPRRCSLE QRTKELDSRF LQLVHGGLPA RPSYMIARPP RPVRGLCSSR
160 170 180 190 200
NGSLAQFGQG YCYLSAIVDS ARWRVARTTG WCVRVADYLR LLQWVGRRSF
210 220 230 240 250
GSFQIEKSAV DHVYHVVVDA EYQSEQDGAL FYQAILGLAE KDPLARIGGR
260 270 280 290 300
LNPLAAEFAP GSALRVEPVT PQVTRRKGST RMTGRDPTIV SVGKVGMAIT
310 320 330 340 350
SIQDALVATE LRNVNFGRRD TEAECRRLWA RYEVNDYFRR HKAELLKFDA
360 370 380 390 400
RLRSRMAKKP ASSRARPSDA KIQCIGWRDR HLLPQRLAGL SKQGRSLVWS
410 420 430 440 450
RFATSNIRRK TPPCVVNPSA DPVVHNWKDS AALAVKKIAE ARRRQEIRAA
460 470 480 490 500
AYAERAKARG QTNVVASISE AIETTLRRNK TRFALDGLHL AASAIVTTRL
510 520 530 540 550
RSWNQEEIRA GREFRKSTTS WIWRHVPSSI QDALNLTSVR DKLDPGRAFG
560 570 580 590 600
YVQAAVAQGM SDFRRAKRAL AIVAKPVIRN IRDPYEHGFV KRDGKLRHSR
610 620
DAFNKKLRTK AVAATKVHKI KF
Length:622
Mass (Da):69,688
Last modified:May 10, 2005 - v2
Checksum:iAFCB274E2197B732
GO

Sequence cautioni

The sequence CAA32666 differs from that shown. Reason: Frameshift at positions 291 and 608.Curated
The sequence CAA32667 differs from that shown. Reason: Frameshift at positions 291 and 608.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14524 mRNA Translation: CAA32666.1 Frameshift.
X14524 mRNA Translation: CAA32667.1 Frameshift.
M57938 Genomic RNA Translation: AAA67457.1
PIRiS03833
S15009
RefSeqiNP_041090.1, NC_001492.1

Genome annotation databases

GeneIDi1403615
KEGGivg:1403615

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14524 mRNA Translation: CAA32666.1 Frameshift.
X14524 mRNA Translation: CAA32667.1 Frameshift.
M57938 Genomic RNA Translation: AAA67457.1
PIRiS03833
S15009
RefSeqiNP_041090.1, NC_001492.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC07.001

Proteomic databases

PRIDEiP10941

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1403615
KEGGivg:1403615

Phylogenomic databases

OrthoDBiVOG090002CP

Family and domain databases

InterProiView protein in InterPro
IPR002704 Peptidase_C7_dom
PfamiView protein in Pfam
PF01830 Peptidase_C7, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPOLA_CHPVE
AccessioniPrimary (citable) accession number: P10941
Secondary accession number(s): P10942, Q04349
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 10, 2005
Last modified: March 15, 2017
This is version 66 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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