Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
HC-Pro + H2O | tobacco vein mottling 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 | ? | - |
? | |
HC-Pro + H2O | potato virus Y | 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 | zucchini yellow mosaic 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 | ? | - |
? | |
HC-Pro + H2O | Plum pox 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 | ? | - |
? | |
HC-Pro + H2O | barley yellow mosaic 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 | ? | - |
? | |
HC-Pro + H2O | Johnsongrass mosaic 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 | ? | - |
? | |
HC-Pro + H2O | papaya ringspot 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 | ? | - |
? | |
HC-Pro + H2O | Pea seed-borne mosaic 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 | ? | - |
? | |
HC-Pro + H2O | Peanut stripe 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 | ? | - |
? | |
HC-Pro + H2O | pepper mottle 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 | ? | - |
? | |
HC-Pro + H2O | Potato virus Y strain C | 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 | turnip mosaic 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
barley yellow mosaic virus | - |
- |
- |
Johnsongrass mosaic virus | - |
- |
- |
papaya ringspot virus | - |
- |
- |
Pea seed-borne mosaic virus | - |
- |
- |
Peanut stripe virus | - |
- |
- |
pepper mottle virus | - |
- |
- |
Plum pox virus | - |
- |
- |
potato virus Y | - |
- |
- |
Potato virus Y strain C | - |
- |
- |
tobacco vein mottling virus | - |
- |
- |
turnip mosaic virus | - |
- |
- |
zucchini yellow mosaic virus | - |
- |
- |
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 vein mottling virus | ? | - |
? | |
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 | ? | - |
? | |
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 | zucchini yellow mosaic virus | ? | - |
? | |
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 | Plum pox virus | ? | - |
? | |
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 | barley yellow mosaic virus | ? | - |
? | |
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 | Johnsongrass mosaic virus | ? | - |
? | |
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 | papaya ringspot virus | ? | - |
? | |
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 | Pea seed-borne mosaic virus | ? | - |
? | |
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 | Peanut stripe virus | ? | - |
? | |
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 | pepper mottle virus | ? | - |
? | |
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 strain C | ? | - |
? | |
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 | turnip mosaic virus | ? | - |
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