Substrates for peptidase C04.014: potato virus A NIa peptidase

Summary Alignment Sequences Sequence features Distribution Literature Substrates

Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are thought to be pathologically relevant are indicated by D. Peptide and protein substrates that are not physiologically relevant are indicated by N. Synthetic substrates are indicated by S. Click on the symbol to show only physiological, non-physiological or synthetic substrates, or here to display all substrates. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a protein substrate, click on the UniProt Accession.

Substrate	Uniprot	Residue range	Cleavage Site	Cleavage type	Evidence	P4	P3	P2	P1	P1'	P2'	P3'	P4'	Reference
polyprotein	Q9DIC2	1-3059	peptide-Gln1102+Ala-peptide	P	NT	Val	Leu	Phe	Gln	Ala	Lys	Ala	Ser	Merits et al., 2002
polyprotein	Q9DIC2	1-3059	peptide-Gln1154+Ser-peptide	P	NT	Val	Gln	Phe	Gln	Ser	Leu	Asp	Asp	Merits et al., 2002
polyprotein	Q9DIC2	1-3059	peptide-Gln1789+Ser-peptide	P	NT	Val	Gln	Phe	Gln	Ser	Gly	Thr	Gln	Merits et al., 2002
polyprotein	Q9DIC2	1-3059	peptide-Gln1842+Gly-peptide	P	NT	Val	Ala	Phe	Gln	Gly	Tyr	Asn	Lys	Merits et al., 2002
polyprotein	Q9DIC2	1-3059	peptide-Glu2031+Ser-peptide	P	NT	Val	Glu	Phe	Glu	Ser	Thr	Ser	Met	Merits et al., 2002
polyprotein	Q9DIC2	1-3059	peptide-Gln2274+Gly-peptide	P	NT	Val	Tyr	Thr	Gln	Gly	Cys	Asp	Ser	Merits et al., 2002
polyprotein	Q9DIC2	1-3059	peptide-Gln2790+Ala-peptide	P	NT	Val	Tyr	Phe	Gln	Ala	Glu	Thr	Leu	Merits et al., 2002