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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Subunits
Subunits on EC 3.4.22.45 - helper-component proteinase
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dimer
additional information
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nested deletion and domain mapping for enzyme analysis, overview
?
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x * 99000, recombinant MBP-tagged wild-type enzyme, SDS-PAGE
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present as a homodimer. The ability to dimerize may be important for aphid transmission, but less so for the other functions of the protein
dimer
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2 * 53000, the enzyme is a dimer in solution, the N-terminus is not essential for self-interaction, SDS-PAGE
dimer
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present as a homodimer. The ability to dimerize may be important for aphid transmission, but less so for the other functions of the protein