Literature summary for 3.4.22.45 extracted from

Boonrod, K.; Fuellgrabe, M.W.; Krczal, G.; Wassenegger, M.
Analysis of the autoproteolytic activity of the recombinant helper component proteinase from zucchini yellow mosaic virus (2011), Biol. Chem., 392, 937-945.

Search for more literature for 3.4.22.45

Cloned(Commentary)

Cloned (Comment)	Organism
functional expression of wild-type MBP:HA-HC-Pro:GFP and truncated mutant MBP:HA-HC-Pro:GFP N1, i.e. enzyme tagged with HA, GFP, and maltose-binding protein, in Escherichia coli leads to autoproteolytic cleavage of the green fluorescent protein, GFP	zucchini yellow mosaic virus

Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of the first 93 residues of the N-terminus of ZYMV HC-Pro. Mutation of the conserved Gly456 residue does not affect the autoproteolytic activity of ZYMV HC-Pro	zucchini yellow mosaic virus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
126000	-	recombinant MBP:HA-HC-Pro:GFP	zucchini yellow mosaic virus

Organism

Organism	UniProt	Comment	Textmining
zucchini yellow mosaic virus	-	ZYMV	-

Synonyms

Synonyms	Comment	Organism
HC-Pro	-	zucchini yellow mosaic virus
helper component proteinase	-	zucchini yellow mosaic virus

General Information

General Information	Comment	Organism
evolution	amino acids essential for the proteolytic activity of ZYMV HC-Pro are distinct from those of the tobacco etch virus HC-Pro, although the amino acid sequences in the proteolytic active domain are conserved among potyviruses	zucchini yellow mosaic virus
physiological function	besides its RNA silencing suppressor, RSS, activity, HC-Pro also exhibits protease, the multifunctional helper component proteinase of potyviruses contains an autoproteolytic function that, together with the protein 1 and NIa proteinase, EC 3.4.22.44, processes the polyprotein into mature proteins	zucchini yellow mosaic virus

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Release 2023.1 (January 2023)