3.4.22.28: picornain 3C
This is an abbreviated version!
For detailed information about picornain 3C, go to the full flat file.
Word Map on EC 3.4.22.28
-
3.4.22.28
-
polyproteins
-
capsid
-
picornaviruses
-
non-structural
-
3c-like
-
rupintrivir
-
positive-sense
-
picornaviridae
-
rhinoviruses
-
encephalomyocarditis
-
enteroviruses
-
fmdv-specific
-
noroviruses
-
vp3
-
gln-gly
-
medicine
-
drug development
-
shutoff
-
molecular biology
- 3.4.22.28
- polyproteins
-
capsid
- picornaviruses
-
non-structural
-
3c-like
- rupintrivir
-
positive-sense
- picornaviridae
- rhinoviruses
-
encephalomyocarditis
- enteroviruses
-
fmdv-specific
- noroviruses
- vp3
- gln-gly
- medicine
- drug development
-
shutoff
- molecular biology
Reaction
Selective cleavage of Gln-/-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly =
Synonyms
3C protease, 3C protein, 3C proteinase, 3C-like protease, 3C-protease, 3CL, 3cLpro, 3CP, 3Cpro, 3Cpro protease, Avihepatovirus 3C protease, coxsackievirus 3C proteinase, cysteine proteinase 3C, DHAV 3C protease, enterovirus 3C protease, EV71 3Cpro, foot-and-mouth protease 3C, HAC 3C, HAV 3C protease, HAV 3Cpro, hepatitis A virus 3C proteinase, HRV 3C protease, HRV 3Cpro, HRV type-14 3C protease, HRV16 3C protease, Human rhinovirus 3C protease, human rhinovirus type-14 3C protease, nonstructural 3 protease, NS3 protease, NS6 protease, P3C, picornain 3C, picornain-3C, picornaviral 3C protease, picornavirus endopeptidase 3C, poliovirus protease 3C, poliovirus proteinase 3C, protease 3C, proteinase, foot-and-mouth-disease virus, 3C, proteinase, picornavirus, 3C, proteinase, poliovirus, 3C, proteinase, rhinovirus, 3C, rhinovirus 3C protease, rhinovirus protease 3C, SAT-type 3C protease, Senecavirus A 3C protease, SV3CP, SVA 3Cpro, tomato ringspot nepovirus 3C-related protease
ECTree
3.4.22.28 picornain 3CAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.22.28 - picornain 3C
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR + H2O
(2-(N-methylamino)benzoyl)-IEALFQ + GPPK(2,4-dinitrophenyl)-FR
most efficient substrate
-
-
?
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate + H2O
?
-
slowly turned over
-
-
?
2-(N-methylamino)benzoyl-DEAMEQGVSDYIK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-DEAMEQ + GVSDYIK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-IAALFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IAALFQ + GPPK(2,4-dinitrophenyl)FR
-
-
-
?
2-(N-methylamino)benzoyl-IEAAFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEAAFQ + GPPK(2,4-dinitrophenyl)FR
2-(N-methylamino)benzoyl-IEALAQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEALAQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IEALFQSPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEALFQ + SPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IEALKQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEALKQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IEFLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEFLFQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IELLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IELLFQ + GPPK(2,4-dinitrophenyl)FR
2-(N-methylamino)benzoyl-LFAGFQGAYSGAK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-LFAGFQ + GAYSGAK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-QTGTIQGDRVADK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-QTGTIQ + GDRVADK-2,4-dinitrophenyl
poor substrate
-
-
?
2-(N-methylamino)benzoyl-RQAVTQGFPTELK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-RQAVTQ + GFPTELK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-RTATVQGPSLDFK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-RTATVQ + GPSLDFK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-TSAVLQSGFRK-(2,4-dinitrophenyl)-Met + H2O
2-(N-methylamino)benzoyl-TSAVLQ + SGFRK-(2,4-dinitrophenyl)-Met
-
-
-
?
2-aminobenzoic acid-Phe-Thr-Gln-Ser-Glu-Gly-Glu-Phe(NO2)-Ala + H2O
?
-
poor substrate
-
-
?
2-aminobenzoyl-AALFQGPLQ-EDDnp + H2O
2-aminobenzoyl-AALFQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EAAFQGPLQ-EDDnp + H2O
2-aminobenzoyl-EAAFQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALAQGPLQ-EDDnp + H2O
2-aminobenzoyl-EALAQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQAPLQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + APLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQGALQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GALQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQGPAQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GPAQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQGPLQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-Nle-Nle-Nle-Glu-Ala-Leu-Phe-Gln-Gly-Pro-(4-nitro)Phe + H2O
2-aminobenzoyl-Nle-Nle-Nle-Glu-Ala-Leu-Phe-Gln + Gly-Pro-(4-nitro)Phe
-
synthetic peptide spanning the 2C/3A cleavage region of poliovirus polyprotein
-
?
4-(4-dimethylaminophenylazo)benzoic acid-KTSAVLQSGFRKME-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoic acid-KTSAVLQ + SGFRKME-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
fluorogenic substrate
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-ASFMNQSKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-ASFMNQ + SKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid
YP_007969882
the fluorometric substrate is cleaved by the 3C protease at the 2C-3A junction, which is derived from the native protease cleavage site within the DHAV polyprotein
-
-
?
Ac-RHSVGATLEALFQGPPVYREIKIS-NH2 + H2O
Ac-RHSVGATLEALFQ + GPPVYREIKIS-NH2
-
-
-
-
?
acetyl-Arg-Ser-Tyr-Phe-Ala-Gln-Ile-Gln-Gly-Glu-Ile-Gln-Trp-Met-Arg-Pro-NH2 + H2O
acetyl-Arg-Ser-Tyr-Phe-Ala-Gln-Ile-Gln + Gly-Glu-Ile-Gln-Trp-Met-Arg-Pro-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3C/3D
-
?
acetyl-Asn-Cys-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Asn-Cys-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 2C/3A
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Gly-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Gly-NH2
-
as good as acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-NH2
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-NH2
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
-
sequence corresponding to 2C/3A cleavage site of polyprotein
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + NH3
-
cleavage with reduced but significant efficiency, better substrate than acetyl-Glu-Ala-Leu-Phe-Gln-Gly-NH2
-
?
acetyl-Glu-Ile-Pro-Tyr-Ala-Ile-Glu-Gln-Gly-Asp-Ser-Trp-Leu-Lys-Lys-Phe-NH2 + H2O
acetyl-Glu-Ile-Pro-Tyr-Ala-Ile-Glu-Gln + Gly-Asp-Ser-Trp-Leu-Lys-Lys-Phe-NH2
-
best substrate, corresponding to poliovirus type 2 polyprotein cleavage site 2B/2C
-
?
acetyl-Ile-Arg-Thr-Ala-Lys-Val-Gln-Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2 + H2O
acetyl-Ile-Arg-Thr-Ala-Lys-Val-Gln + Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3B/3C
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
acetyl-Thr-Ile-Arg-Thr-Ala-Lys-Val-Gln-Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2 + H2O
acetyl-Thr-Ile-Arg-Thr-Ala-Lys-Val-Gln + Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3B/2C
-
?
acetyl-Tyr-Glu-Glu-Glu-Ala-Met-Glu-Gln-Gly-Ile-Ser-Asn-Tyr-Ile-Glu-Ser-NH2 + H2O
acetyl-Tyr-Glu-Glu-Glu-Ala-Met-Glu-Gln + Gly-Ile-Ser-Asn-Tyr-Ile-Glu-Ser-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 2A/2B
-
?
acetyl-Tyr-Lys-Leu-Phe-Ala-Gly-His-Gln-Gly-Ala-Tyr-Thr-Gly-Leu-Phe-Asn-NH2 + H2O
acetyl-Tyr-Lys-Leu-Phe-Ala-Gly-His-Gln + Gly-Ala-Tyr-Thr-Gly-Leu-Phe-Asn-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3A/3B
-
?
Asp-Ser-Leu-Glu-Thr-Leu-Phe-Gln-Gly-Pro-Val-Tyr-Lys-Asp-Leu-Glu + H2O
Asp-Ser-Leu-Glu-Thr-Leu-Phe-Gln + Gly-Pro-Val-Tyr-Lys-Asp-Leu-Glu
-
represents 2C/3A cleavage site, wild-type and E71D, D85N, K155E mutants, not other mutants
-
?
CstF-64 protein + H2O
?
-
CstF-64 protein is short for cleavage stimulation factor, 39 pre-RNA, subunit 2, 64 kD. The 3Cpro cleavage sites are located at position 251 in the N-terminal P/G-rich domain and at multiple positions close to the C-terminus of CstF-64 (around position 500)
-
-
?
Dabcyl-APAKQLLD(Edans)FDLLK + H2O
Dabcyl-APAKQ + LLD(Edans)FDLLK
-
-
-
-
?
Dabcyl-GLRTQSFS-EDANS + H2O
?
-
fluorogenic substrate, hydrolysis at the glutamine residue
-
-
?
Dabcyl-IEALFQGPPKFRE-Edans + H2O
Dabcyl-IEALFQ + GPPKFRE-Edans
-
-
-
?
Dabcyl-RTATVQGPSLDFE-EDANS + H2O
Dabcyl-RTATVQ + GPSLDFE-EDANS
-
-
-
?
Dabcyl-RTATVQGPSLDFKE-Edans + H2O
Dabcyl-RTATVQ + GPSLDFKE-Edans
-
-
-
?
Dabcyl-TSAVLQSGFRKM-Edans + H2O
Dabcyl-TSAVLQ + SGFRKM-Edans
poor substrate
-
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
eIF4GI + H2O
?
-
cleavage in baby hamster kidney cells and 3T3 cells, cleavage can occur either on the full-length protein or on the primary cleavage product that is generated by Lpro, human and green monkey eIF4GI is resistant to the action of 3Cpro, a single amino acid substitution renders human eIF4GI sensitive to 3Cpro
-
-
?
encephalomyocarditis virus polyprotein + H2O
?
-
cleavage sites: Gln-Gly, Glu-Ser and Glu-Ala
-
-
?
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
-
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
-
-
?
foot-and-mouth-disease virus P1 precursor polyprotein + H2O
mature structural foot-and-mouth-disease virus proteins
-
recombinant foot-and-mouth-disease virus enzyme, cleaves VP3-VP1 site, followed by VP0-VP3 and VP1-2A site (least efficiently), kinetic of P1 processing
VPO-VP3 + VP1-2A (enzyme from supernatant), VPO + VP3 + VP1 (pellet enzyme)
?
foot-and-mouth-disease virus P1-2A polyprotein + H2O
mature structural foot-and-mouth-disease virus proteins
-
recombinant foot-and-mouth-disease virus enzyme, cleaves VP3-VP1 site initially, followed by VP0-VP3 and VP1-2A site (least efficiently), kinetic of P1-processing
VPO-VP3 + VP1-2A (enzyme from supernatant), VPO + VP3 + VP1 (pellet enzyme)
?
foot-and-mouth-disease virus P2 precursor protein + H2O
foot-and-mouth-disease virus protein 2B + foot-and-mouth-disease virus protein 2C + foot-and-mouth-disease virus protein 2A-2B
-
-
-
?
Glu-Ala-Ile-Ala-Glu-Glu-Gln-Gly-Leu-Ser-Asp-Tyr-Ile-Thr + H2O
?
-
synthetic peptide spanning the 2A/2B cleavage region of human rhinovirus polyprotein
-
-
?
Glu-Ala-Leu-Phe-Gln-4-nitroanilide + H2O
Glu-Ala-Leu-Phe-Gln + 4-nitroaniline
-
-
-
-
?
Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O
Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
-
represents 2C/3A cleavage site, wild-type and C147S mutant, the latter with very reduced activity
-
?
hepatitis A virus deltaP1-2AB polyprotein fragment + H2O
hepatitis A virus protein 2A + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2BC + hepatitis A virus protein 2 + hepatitis A virus protein 2B
-
C-terminally truncated protein
-
?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O
hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
hepatitis A virus deltaVP1-P2-P3*my polyprotein fragment + H2O
hepatitis A virus protein 2BC + hepatitis A virus proteins P3*my + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
C-terminally truncated protein, proteolytically inactive substrate, kinetics, yields the same products as active polyprotein precursor deltaVP1-P2-P3*
P3my and deltaVP1-2A are intermediates
?
hepatitis A virus P1-2AB* polyprotein fragment + H2O
hepatitis A virus protein VP3 + hepatitis A virus proteins VP0 + hepatitis A virus proteins VP1-2A + hepatitis A virus proteins VP0-VP3 + hepatitis A virus proteins P1-2A + hepatitis A virus proteins 2A
-
C-terminally truncated protein, cleavage sites: VPO/VP3, VP3/VP1, 2A/2B, less efficient are VP1/2A and 2B/2C, via 2BC
-
?
hepatitis A virus P1-2ABC* polyprotein fragment + H2O
hepatitis A virus protein VP3 + hepatitis A virus proteins VP0 + hepatitis A virus proteins VP1-2A + hepatitis A virus proteins VP0-VP3 + hepatitis A virus proteins P1-2A + hepatitis A virus proteins 2A + hepatitis A virus proteins 2BC
-
C-terminally truncated protein, cleavage sites: VPO/VP3, VP3/VP1, 2A/2B, less efficient are VP1/2A and 2B/2C, via 2BC
-
?
hepatitis A virus P1-P2 precursor polyprotein + H2O
hepatitis A virus protein 2A + hepatitis A virus protein 2B + hepatitis A virus protein 2C + hepatitis A virus protein 3ABC + hepatitis A virus protein 3D
-
most effective cleavage at 2A/2B and 2C/3A sites
via respective intermediate products
?
hepatitis A virus P2-P3 precursor polyprotein + H2O
?
-
trans-cleavage, rapid cleavage at P2/P3 junction, the 3A/3B, 3B/3C and 3C/3D sites are less efficiently cleaved, the hepatitis A virus enzyme has a broader activity profile than enzymes of other picornaviruses, recombinant enzyme cleaves all putative cleavage sites of the polyprotein
-
-
?
hepatitis A virus polyprotein + H2O
hepatitis A virus protein P1-2A + hepatitis A virus protein P3 + hepatitis A virus protein 2BC + hepatitis A virus protein 3D + hepatitis A virus protein 3ABC
-
cleavage of P2-P3 domain, cleaves primary cleavage site and all secondary sites within P2 as well as the 3C/3D junction
followed by hepatitis A virus protein 2B and hepatitis A virus protein 2C and later by hepatitis A virus protein VP0 and hepatitis A virus protein VP3, enzyme-concentration dependent product formation
?
histone protein H3 + H2O
?
-
in BHK-cells, foot-and-mouth-disease virus enzyme
-
-
?
host zinc-finger antiviral protein + H2O
?
-
cleavage specifically at Gln369, ZAP cleavage is dependent on its amino acid pair Q369 and G370
-
-
?
human rhinovirus 3CD polyprotein fragment + H2O
?
-
recombinant enzyme HRV-14, structure/mechanism study
-
-
?
in vitro-translated (35S)methionine-labeled transcription factor cyclic AMP-responsive element binding protein + H2O
?
-
-
-
-
?
interferon regulatory factor 7 + H2O
?
-
cleavage occurs at the Q189-S190 junction within the constitutive activation domain
-
-
?
L-P1-2A precursor polypeptide of encephalomyocarditis virus + H2O
peptide P1-2A
-
cardioviruses
-
?
Lys-Gly-Leu-Phe-Ser-Gln-Ala-Lys-Ile-Ser-Leu-Phe-Tyr-Thr + H2O
Lys-Gly-Leu-Phe-Ser-Gln + Ala-Lys-Ile-Ser-Leu-Phe-Tyr-Thr
-
-
-
?
mitochondrial antiviral signaling protein + H2O
?
-
3Cpro-mediated MAVS cleavage occurs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling
-
-
?
N-acetyl-DEFQLQ-4-nitroanilide + H2O
N-acetyl-DEFQLQ + 4-nitroaniline
-
-
-
-
?
nuclear factor-kappaB essential modulator + H2O
?
-
the enzyme cleaves the substrate at the Q304 residue, negating its signaling adaptor function
-
-
?
P1-2A precursor polypeptide of encephalomyocarditis virus + H2O
peptide P1 + peptide 2A
-
cardio- and aphthoviruses
-
?
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
poly(A) binding protein + H2O
?
-
the enzyme cleaves poly(A) binding protein within the C-terminal domain at Q437/G438
-
-
?
poly(A) binding protein + H2O
fragments of poly(A) binding protein
-
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
-
-
?
Poly(A)-binding protein + H2O
?
-
3Cpro removes the C-terminal domain that interacts with several translation factors, in HeLa cells 3Cpro inhibits translation of endogenous mRNAs and reporter RNA, 3Cpro-mediated translation inhibition can be restored by the addition of exogenous poly(A)-binding protein
-
-
r
poly(A)-binding protein + H2O
fragments of poly(A)-binding protein
-
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
-
-
?
polypeptide translated from plasmid DNA T7-delta3A-3B-3Cmut-delta3D
delta3A-3B-3Cmut + 3Cmut-delta3D + 3B-3Cmut-delta3D
-
-
-
-
?
Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O
fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
-
-
-
-
?
Thr-Gly-Leu-Phe-Gln-Gly-Pro + H2O
Thr-Gly-Leu-Phe-Gln + Gly-Pro
-
-
-
-
?
Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O
?
-
3Cpro cleaves both the N- and C-terminal domains of TRIF and localizes with TRIF to signalosome complexes within the cytoplasm
-
-
?
2-(N-methylamino)benzoyl-IEAAFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEAAFQ + GPPK(2,4-dinitrophenyl)FR
-
-
-
?
2-(N-methylamino)benzoyl-IEAAFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEAAFQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IELLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IELLFQ + GPPK(2,4-dinitrophenyl)FR
-
-
-
?
2-(N-methylamino)benzoyl-IELLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IELLFQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to amino acid sequence flanking 2C/3A cleavage site, wild-type and mutant D85N enzyme
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 2C/3A
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to amino acid sequence flanking 2C/3A cleavage site, wild-type and mutant D85N enzyme
-
?
activated transcription factor TFIIIC + H2O
?
-
in HeLa-cells, poliovirus enzyme
-
-
?
activated transcription factor TFIIIC + H2O
?
-
in HeLa-cells, poliovirus enzyme, involved in shut-off of host-cell transcription
-
-
?
Dabcyl-KEALFQGPPQFE-Edans + H2O
Dabcyl-KEALFQ + GPPQFE-Edans
-
best substrate
-
-
?
Dabcyl-KEALFQGPPQFE-Edans + H2O
Dabcyl-KEALFQ + GPPQFE-Edans
-
best substrate
-
-
?
Dabcyl-KIGNTIEALFQGPPKFRE-EDANS + H2O
Dabcyl-KIGNTIEALFQ + GPPKFRE-EDANS
-
-
-
-
?
Dabcyl-KIGNTIEALFQGPPKFRE-EDANS + H2O
Dabcyl-KIGNTIEALFQ + GPPKFRE-EDANS
-
-
-
-
?
Dabcyl-KRTATVQGPSLDFE-Edans + H2O
Dabcyl-KRTATVQ + GPSLDFE-Edans
-
-
-
?
Dabcyl-KRTATVQGPSLDFE-Edans + H2O
Dabcyl-KRTATVQ + GPSLDFE-Edans
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVL + QSGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
-
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
-
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
-
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
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 2.93
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 2.7
-
-
?
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 4.45
-
-
?
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 4.11
-
-
?
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 3.79
-
-
?
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 3.65
-
-
?
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 18.65
-
-
?
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 14.22
-
-
?
FAGLRQAVKQGFPTEL + H2O
FAGLRQAVKQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.902
-
-
?
FAGLRQAVKQGFPTEL + H2O
FAGLRQAVKQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.902
-
-
?
FAGLRQAVKQGIPTEL + H2O
FAGLRQAVKQ + GIPTEL
-
cleavage efficacy (micromol/l/min): 0.3
-
-
?
FAGLRQAVKQGIPTEL + H2O
FAGLRQAVKQ + GIPTEL
-
cleavage efficacy (micromol/l/min): 0.3
-
-
?
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
-
cleavage efficacy (micromol/l/min): 5.77
-
-
?
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
-
reference peptide, cleavage efficacy (micromol/l/min): 5.08
-
-
?
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.27
-
-
?
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.21
-
-
?
Foot-and-mouth disease virus polyprotein + H2O
?
-
3Cpro is only weakly selective for Gln over Glu, most susceptible peptides correspond to the VP1/2A and 2B/2C junctions, which were completely cleaved within 6 hours, whereas peptides corresponding to the VP2/VP3, 2C/3A, 3A/3B1, 3B1/3B2 and 3B2/3B3 junctions were uncleaved after 24 hours incubation
-
-
?
Foot-and-mouth disease virus polyprotein + H2O
?
-
3Cpro is only weakly selective for Gln over Glu, most susceptible peptides correspond to the VP1/2A and 2B/2C junctions, which were completely cleaved within 6 hours, whereas peptides corresponding to the VP2/VP3, 2C/3A, 3A/3B1, 3B1/3B2 and 3B2/3B3 junctions were uncleaved after 24 hours incubation
-
-
?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O
hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
putative primary cleavage sites within P2 region are VP1-2A, 2A/2B, i.e. Gln745-Ser and Gln836-Ala
-
-
?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O
hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
deltaVP1-P2-P3*, C-terminally truncated protein
-
?
hepatitis A virus polyprotein + H2O
?
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
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
-
-
?
hepatitis A virus polyprotein + H2O
?
-
processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner
-
-
?
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
-
-
?
hepatitis A virus polyprotein + H2O
?
-
the enzyme is responsible for the processing of the viral polyprotein
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
-
cleavage efficacy (micromol/l/min): 10.72
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
-
cleavage efficacy (micromol/l/min): 8.37
-
-
?
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
-
cleavage efficacy (micromol/l/min): 0.063
-
-
?
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
-
cleavage efficacy (micromol/l/min): 0.055
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
-
cleavage efficacy (micromol/l/min): 4.3
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
-
cleavage efficacy (micromol/l/min): 4.1
-
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ + GEIQWM
-
cleavage efficacy (micromol/l/min): 5.09
-
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ + GEIQWM
-
cleavage efficacy (micromol/l/min): 5.01
-
-
?
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
-
cleavage efficacy (micromol/l/min): 9.78
-
-
?
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
-
cleavage efficacy (micromol/l/min): 8.26
-
-
?
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
-
cleavage efficacy (micromol/l/min): 0.23
-
-
?
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
-
cleavage efficacy (micromol/l/min): 0.22
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
-
-
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
most maturation cleavages within the precursor polyprotein are mediated by the enzyme
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
essential for processing of virus polyprotein containing structural proteins and enzymes including the protease 3C itself
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
the enzyme is essential for viral replication and infectivity
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
-
in-cis cleavage, autocatalytical processing, cleavage sites: 3A/3B and 3B/3C, in-cis cleavage ability of D85N mutant severely impaired
poliovirus protein 3B is only 22 amino acids long and not detected in the assay
?
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
-
in-cis cleavage, autocatalytical processing, cleavage sites: 3A/3B and 3B/3C, in-cis cleavage ability of D85N mutant severely impaired
poliovirus protein 3B is only 22 amino acids long and not detected in the assay
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
exclusive cleavage site: Gln-Gly
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
cleavage map
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
initial cleavage at 2C-3A and 2B-2C, followed by 3A-3B and/or 3C-3D
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
proteolytic autocatalysis
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
protease 2A cleavage at COOH-terminal Tyr-Gly bond of P1, i.e. P1/P2 junction, may be necessary before this region of the polyprotein serves as substrate for protease 3C
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
essential for processing of virus polyprotein containing strucutral proteins and enzymes including the protease 3C itself
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
the polyprotein is cleaved into mature proteins predominantly by the viral 3C protease
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
protease 2A cleavage at COOH-terminal Tyr-Gly bond of P1, i.e. P1/P2 junction, may be necessary before this region of the polyprotein serves as substrate for protease 3C
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein fragment corresponding to 2BC coding region + H2O
?
-
in-trans cleavage, wild-type and mutant D85N enzyme
-
-
?
poliovirus polyprotein fragment corresponding to 2BC coding region + H2O
?
-
in-trans cleavage, wild-type and mutant D85N enzyme
-
-
?
receptor-interacting protein kinase 1 + H2O
?
-
cleavage of the RIPK1 death-domain, and generation of N-terminal RIPK1 fragments
-
-
?
receptor-interacting protein kinase 1 + H2O
?
-
in vitro cleavage of RIPK1 by 3Cpro in HeLa cell extracts, cleavage of the RIPK1 death-domain, and generation of N-terminal RIPK1 fragments. The middle p62/SQSTM1 binding domain of RIPK1 contains three strictly defined HRV 3Cpro consensus motifs [AVNTPISQ]-x-x-Q-[GNSA]-[PLDIQEVAN] at Q401, Q464, and Q573. 3Cpro cleaves parts of the middle domain and the C-terminus of RIPK1. Enzyme 3Cpro generates a 60 kDa N-terminal RIPK1 fragment
-
-
?
receptor-interacting protein kinase-1 + H2O
?
i.e. RIPK1, HRV 3C protease cleaves RIPK1 to produce a 23 kDa cleavage product
-
-
?
transcription factor OCT-1 + H2O
?
-
cleaved by 3Cpro, precursor 3CD and mutant 3CD delta371
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
-
cleavage efficacy (micromol/l/min): 0.63
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
-
cleavage efficacy (micromol/l/min): 0.56
-
-
?
additional information
?
-
YP_007969882
optimization of in vitro cleavage assay method with a fluorogenic peptide substrate derived from the cleavage site of the DHAV polyprotein, overview
-
-
?
additional information
?
-
-
optimization of in vitro cleavage assay method with a fluorogenic peptide substrate derived from the cleavage site of the DHAV polyprotein, overview
-
-
?
additional information
?
-
-
no hydrolysis of acetyl-Glu-Ala-Leu-Phe-Glu-Gly-Pro
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
all catalytic-site mutations result in reduction or inactivation of autocatalytic cleavage of recombinant 3C precursor protein, Cys147 to Ala mutant is inactive, Cys147 to Ser has reduced in-cis and in-trans activity
-
-
?
additional information
?
-
-
cleavage of purified fusion proteins by immobilised protease
-
-
?
additional information
?
-
-
does not cleave death-associated protein 5
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
non-proteolytic function: wild-type and H40D, E71A, C16S mutant enzymes bind specifically to 5'-noncoding region of viral RNA, not D85E or D85N mutant enzymes
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
3Cpro possess RNA-binding activity, the regions responsible for RNA binding are KFRDI (positions 82-86) and VGK (positions 154-156)
-
-
?
additional information
?
-
-
chymotrypsin-like protease is required for viral replication
-
-
?
additional information
?
-
-
picornavirus 3Cpro generally cleaves peptides at the Gln/Gly junction
-
-
?
additional information
?
-
-
usage of a fluorescence resonance energy transfer (FRET)-based enzyme assay for activity determination
-
-
?
additional information
?
-
-
no hydrolysis of acetyl-Arg-Ser-Tyr-Phe-Thr-Gln-Ile-Gln-Gly-Glu-Ile-Gln-Trp-Met-Arg-Pro-NH2
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
does not hydrolyze 4-aminobenzyl-EALFAGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFEGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFRGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFHGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFNGPLQED-2,4-dinitrophenol, and 4-aminobenzyl-EALFYGPLQED-2,4-dinitrophenol
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
the enzyme induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
-
-
?
additional information
?
-
-
the foot-and-mouth disease virus 3Cpro to cleaves sequences containing either P1-Gln or P1-Glu
-
-
?
additional information
?
-
-
the VP2 K217R and VP3 I2P substitutions (near the VP0/VP3 junction of the substrate) strongly reduce the processing at this junction by 3Cpro while the substitution VP2 K217E blocks cleavage. At the VP3/VP1 junction, the substitutions VP3 Q2221P and VP1 T1P each severely inhibit processing at this site. Blocking cleavage at either junction does not prevent processing elsewhere in P1-2A. Processing of the P1-2A precursor in the transient expression assay using BHK cells
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
the pattern of proteolytic products of polyprotein processing in recombinant systems and in infected cells differs, mature protease 3C is produced in bacteria, but cleavage is arrested at 3ABC intermediate in eukaryotic system
-
-
?
additional information
?
-
-
catalytic sites: Cys172 (nucleophile) and His44 (general base), His191 defines Gln-residue specificity
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the accessibility of the HRV 3C cleavage site within RIPK1 in-vitro is probably increased by concurrent cleavage of RIPK1 through caspase-8. Prior to cleavage of RIPK1 by caspase 8 does not abrogate 3C protease-mediated cleavage in vitro
-
-
?
additional information
?
-
-
HRV 3C protease shows high and unique specificity. It recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro and cleaves between glutamine and glycine
-
-
?
additional information
?
-
-
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
-
-
?
