3.4.22.45: helper-component proteinase
This is an abbreviated version!
For detailed information about helper-component proteinase, go to the full flat file.
Word Map on EC 3.4.22.45
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3.4.22.45
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viruses
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potato
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nicotiana
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potyviruses
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polyproteins
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benthamiana
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potyviral
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aphid
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potyviridae
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mottle
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etch
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turnip
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cistron
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plum
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zucchini
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ringspot
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papaya
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nia-pro
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cucurbit
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tritimovirus
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non-persistent
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ipomovirus
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pvyntn
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genome-linked
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rna-silencing
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veinal
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feathery
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agriculture
- 3.4.22.45
- viruses
- potato
- nicotiana
- potyviruses
- polyproteins
- benthamiana
-
potyviral
- aphid
- potyviridae
-
mottle
-
etch
- turnip
-
cistron
- plum
- zucchini
-
ringspot
- papaya
- nia-pro
-
cucurbit
- tritimovirus
-
non-persistent
- ipomovirus
-
pvyntn
-
genome-linked
-
rna-silencing
-
veinal
-
feathery
- agriculture
Reaction
hydrolyses a Gly-/-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-/-Gly, in the processing of the potyviral polyprotein =
Synonyms
HC-Pro, HC-Pro protein, HC-Pro proteinase, HcPro, helper component protease, helper component proteinase, helper component-protease, helper component-proteinase, helper-component proteinase, More, potyvirus helper component proteinase, PVA HC-Pro, strong silencing suppressor P1
ECTree
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.22.45 - helper-component proteinase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the autoproteolytic activity releases its own C-terminus
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
HC-Pro + H2O
?
-
the helper component proteinase HC-Pro is a multifunctional protein with three domains: the N-terminal third contributes to viral replication and aphid transmission, the central domain is required for viral vascular transport, and the C-terminal third contains the proteolytic domain. Proteolytic procession occurs at a Gly-Gly bond at its C-terminus. A Tyr-Xaa-Val-Gly-Gly sequence surrounding the cleavage site is highly conserved. The residues Cys649 and His722 within the proteolytic domain are essential for proteolysis
-
-
?
additional information
?
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-
the enzyme suppresses gene silencing, especially by inhibition of silencing-associated plant smRNA modification at the 2'-hydroxyl of the terminal ribose, and enhancing of 3'-methylation of viral siRNAs, overview
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-
?
additional information
?
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the enzyme is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of posttranscriptional gene silencing
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?
additional information
?
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multifunctional HcPro targets the 20S proteasome and affects its enzymic activities, e.g. in RNA trunover, cell division, signal transduction, and translation, overview
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-
?
additional information
?
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the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
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-
?
additional information
?
-
-
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
?
additional information
?
-
the helper component proteinase of potato virus A interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
?
additional information
?
-
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
?
additional information
?
-
-
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
?
additional information
?
-
the helper component proteinase of potato virus Y interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
-
-
?
additional information
?
-
-
the enzyme is a suppressor of post-transcriptional gene silencing
-
-
?
additional information
?
-
-
the enzyme is essential for viral infection of plants and acts as post-transcriptional gene silencer by interferring with miRNA-controlled developmental pathways
-
-
?
additional information
?
-
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
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-
?
additional information
?
-
the helper component proteinase of tobacco etch virus interacts translation initiation factors with both eIF4E and eIF(iso)4E from Nicotiana tabacum and to a lesser extent from Solanum tuberosum, with interactions with eIF(iso)4E being stronger, analysis by yeast two-hybrid system assay
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-
?
additional information
?
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Tobacco vein mottling potyvirus
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the enzyme is essential for viral infection of plants and acts as post-transcriptional gene silencer by interferring with miRNA-controlled developmental pathways
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-
?
additional information
?
-
-
the enzyme is required for wheat streak mosaic virus transmission by the wheat curl mite, Aceria tosichella, and cannot be replaced by the enzyme of Turnip mosaic virus or Agropyron mosaic virus, while the enzymes of divergent strains function in eriophyd mite transmission assays, overview
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-
?
additional information
?
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conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
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-
?
additional information
?
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conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
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-
?
additional information
?
-
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the helper component-proteinase of the Zucchini yellow mosaic virus inhibits the Arabidopsis thaliana Hua Enhancer 1 methyltransferase, HEN1, activity in vitro
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-
?
additional information
?
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conserved FRNK Box in the helper component proteinase HC-Pro of zucchini yellow mosaic virus identified as a binding region for small RNAs and as a region associated with virus symptoms
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-
?
