EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.22.45 | HC-Pro + H2O |
- |
tobacco vein mottling virus |
? |
- |
? |
3.4.22.45 | HC-Pro + H2O |
- |
tobacco etch virus |
? |
- |
? |
3.4.22.45 | HC-Pro + H2O |
- |
potato virus Y |
? |
- |
? |
3.4.22.45 | HC-Pro + H2O |
- |
zucchini yellow mosaic virus |
? |
- |
? |
3.4.22.45 | HC-Pro + H2O |
- |
Potato virus Y strain C |
? |
- |
? |
3.4.22.45 | HC-Pro + H2O |
- |
lettuce mosaic virus |
? |
- |
? |
3.4.22.45 | HC-Pro + H2O |
- |
potato virus A |
? |
- |
? |
3.4.22.45 | 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 vein mottling virus |
? |
- |
? |
3.4.22.45 | 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 |
? |
- |
? |
3.4.22.45 | 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 |
potato virus Y |
? |
- |
? |