EC Number |
Natural Substrates |
---|
3.4.22.28 | activated transcription factor TFIIIC + H2O |
in HeLa-cells, poliovirus enzyme, involved in shut-off of host-cell transcription |
3.4.22.28 | ERGIC53 protein + H2O |
- |
3.4.22.28 | eukaryotic initiation factor + H2O |
cleaveage at a single site, rabbit eIF5B is proteolytically cleaves during coxsackievirus infection of cultured cells, beginning at 3 h post-infection and increasing thereafter |
3.4.22.28 | eukaryotic initiation factor + H2O |
cleaveage at a single site, rabbit eIF5B is proteolytically cleaves during poliovirus infection of cultured cells, beginning at 3 hours post-infection and increasing thereafter |
3.4.22.28 | foot-and-mouth disease virus capsid precursor (P1-2A) + H2O |
cleavages at the three junctions (VP0/VP3, VP3/VP1, and VP1/2A) within the foot-and-mouth disease virus capsid precursor (P1-2A) by the 3C protease are mutually independent |
3.4.22.28 | hepatitis A virus polyprotein + H2O |
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor |
3.4.22.28 | hepatitis A virus polyprotein + H2O |
involved in primary cleavages yielding precursors of structural proteins, it mediates all secondary cleavages yielding mature structural and functional proteins |
3.4.22.28 | hepatitis A virus polyprotein + H2O |
processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner |
3.4.22.28 | hepatitis A virus polyprotein + H2O |
the enzyme is essential for cleavage of the initially synthesized viral polyprotein precursor to mature fragents and is therefore required for viral replication in vivo |
3.4.22.28 | hepatitis A virus polyprotein + H2O |
the enzyme is responsible for the processing of the viral polyprotein |