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Literature summary for 3.4.22.45 extracted from

  • Kasschau, K.D.; Carrington, J.C.
    Requirement for HC-Pro processing during genome amplification of tobacco etch potyvirus (1995), Virology, 209, 268-273.
    View publication on PubMed
Search for more literature for 3.4.22.45

Protein Variants

Protein Variants Comment Organism
C649S active site mutant, no activity tobacco etch virus
C694S mutant is proteolytically active and capable of cell-to-cell and long-distance movements tobacco etch virus
D715E mutant is proteolytically active and capable of cell-to-cell and long-distance movements tobacco etch virus
H722S active site mutant, no activity tobacco etch virus
S610T mutant is proteolytically active and capable of cell-to-cell and long-distance movements tobacco etch virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
HC-Pro + H2O tobacco etch virus 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 ?
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Organism

Organism UniProt Comment Textmining
tobacco etch virus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 tobacco etch virus ?
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