Substrates for peptidase M04.006: Msp peptidase (Legionella-type)

Summary Alignment Tree 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 CutDB MERNUM
Ac-Ser-Lys-Gly-Pya-NPh-Gly-Gly-Lys-NH2 Ac-Ser-Lys-Gly-Pya+NPh-Gly-Gly-Lys-NH2 S Ser Lys Gly Pya NPh Gly Gly Lys Poras et al., 2012
Ac-Ser-Lys-Gly-Pya-Tyr(NO2)-Gly-Gly-Lys-NH2 Ac-Ser-Lys-Gly-Pya+Tyr(NO2)-Gly-Gly-Lys-NH2 S Ser Lys Gly Pya Tyn Gly Gly Lys Poras et al., 2012
Ac-Ser-Lys-Gly-Pya-Tyr(NO2)-hArg-NH2 Ac-Ser-Lys-Gly-Pya+Tyr(NO2)-hArg-NH2 S Ser Lys Gly Pya Tyn HAr NH2 - Poras et al., 2012
Ac-Ser-Lys-Gly-Pya-Tyr(NO2)-Orn-NH2 Ac-Ser-Lys-Gly-Pya+Tyr(NO2)-Orn-NH2 S Ser Lys Gly Pya Tyn Orn NH2 - Poras et al., 2012
glycerophospholipid:cholesterol acyltransferase Q5DJS6 31-412 peptide-Asn362+Tyr-peptide P MS Phe Ala Arg Asn Tyr Val Leu Gln Lang et al., 2012
glycerophospholipid:cholesterol acyltransferase Q5DJS6 31-412 peptide-Gln366+Tyr-peptide P MS Tyr Val Leu Gln Tyr Thr Gln Val Lang et al., 2012
glycerophospholipid:cholesterol acyltransferase Q5DJS6 31-412 peptide-Gln372+Tyr-peptide P MS Gln Val Leu Gln Tyr Arg Asp Lys Lang et al., 2012
MeOSuc-Arg-Pro-Tyr-NHPhNO2 MeOSuc-Arg-Pro-Tyr+NHPhNO2 S MSu Arg Pro Tyr NAN - - - Woessner, 2004