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activated transcription factor TFIIIC + H2O
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in HeLa-cells, poliovirus enzyme, involved in shut-off of host-cell transcription
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ERGIC53 protein + H2O
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eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
foot-and-mouth disease virus capsid precursor (P1-2A) + H2O
foot-and-mouth disease virus protein VP0 + foot-and-mouth disease virus protein VP3 + foot-and-mouth disease virus protein VP1 + foot-and-mouth disease virus protein 2A
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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
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hepatitis A virus polyprotein + H2O
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host zinc-finger antiviral protein + H2O
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cleavage specifically at Gln369, ZAP cleavage is dependent on its amino acid pair Q369 and G370
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interferon regulatory factor 7 + H2O
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cleavage occurs at the Q189-S190 junction within the constitutive activation domain
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membrin + H2O
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mitochondrial antiviral signaling protein + H2O
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3Cpro-mediated MAVS cleavage occurs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling
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nuclear factor-kappaB essential modulator + H2O
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the enzyme cleaves the substrate at the Q304 residue, negating its signaling adaptor function
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
poly(A) binding protein + H2O
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the enzyme cleaves poly(A) binding protein within the C-terminal domain at Q437/G438
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poly(A) binding protein + H2O
fragments of poly(A) binding protein
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contains 2 main cleavage sites for 3C proteinase within the proline-rich linker domain, cleavage of recombinant protein with 3C proteinase heavily favors the 3Cpro primary cleavage site Q537/G538 over the 3CAlt cleavage site Q413/T414
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poly(A)-binding protein + H2O
fragments of poly(A)-binding protein
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inhibition of viral internal ribosome entry site-mediated translation, cleavage of poly(A)-binding protein by 3Cpro is a necessary component for host translation shutoff
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Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O
fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
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receptor-interacting protein kinase 1 + H2O
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cleavage of the RIPK1 death-domain, and generation of N-terminal RIPK1 fragments
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receptor-interacting protein kinase-1 + H2O
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i.e. RIPK1
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Thr-Gly-Leu-Phe-Gln-Gly-Pro + H2O
Thr-Gly-Leu-Phe-Gln + Gly-Pro
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Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O
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3Cpro cleaves both the N- and C-terminal domains of TRIF and localizes with TRIF to signalosome complexes within the cytoplasm
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TRIF protein + H2O
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additional information
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eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
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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
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eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
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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
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hepatitis A virus polyprotein + H2O
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the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
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hepatitis A virus polyprotein + H2O
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involved in primary cleavages yielding precursors of structural proteins, it mediates all secondary cleavages yielding mature structural and functional proteins
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hepatitis A virus polyprotein + H2O
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processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner
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hepatitis A virus polyprotein + H2O
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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
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hepatitis A virus polyprotein + H2O
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the enzyme is responsible for the processing of the viral polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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most maturation cleavages within the precursor polyprotein are mediated by the enzyme
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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essential for processing of virus polyprotein containing structural proteins and enzymes including the protease 3C itself
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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the enzyme is essential for viral replication and infectivity
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
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involved in proteolytic processing of virus polyprotein
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poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
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essential for processing of virus polyprotein containing strucutral proteins and enzymes including the protease 3C itself
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poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
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the polyprotein is cleaved into mature proteins predominantly by the viral 3C protease
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poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
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involved in proteolytic processing of poliovirus polyprotein
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poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
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involved in proteolytic processing of poliovirus polyprotein
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additional information
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chymotrypsin-like protease is required for viral replication
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additional information
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the enzyme induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
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additional information
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3C protein and 3C-containing precursor proteins play roles in the virus lifecycle before, during and after RNA synthesis, enzyme has uridylylation activity on Vpg peptide
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additional information
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NF-kappaB-p65 activation by SVA 3Cpro. NF-kappaB-p65 cleavage occurs at the caspase cleavage site (444LQFDTDED), suggesting that cleavage of NF-kappaB-p65 is mediated by caspases and not by the direct action of SVA 3Cpro. While expression of wild-type SVA 3Cpro results in activation of Casp-3 and cleavage of NF-kappaB-p65, expression of the 3Cpro catalytic-dead mutants H47D or C159R does not lead to Casp-3 activation nor to NF-kappaB-p65 cleavage
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