Peptidase_C97 |
---|
PFAM accession number: | PF05903 |
---|---|
Interpro abstract (IPR008580): | The PPPDE superfamily (after Permuted Papain fold Peptidases of DsRNA viruses and Eukaryotes), consists of thiol peptidases with a circularly permuted papain-like fold. They contain a PPPDE domain which is a cysteine isopeptidase that exhibits a deSUMOylase activity in PPPDE2 (DeSI-1) and a deubiquinating activity in PPPDE1 (DeSI-2) and is described as a mixed alpha/beta-fold composed of six beta-strands and six alpha-helices. The catalytic dyad is formed by a conserved N-terminal histidine residue on beta2-strand and a conserved C-terminal cysteine residue on the following alpha3-helix (the H-C configuration). This catalytic dyad is invariably conserved in the PPPDE family of proteins [ (PUBMED:15483401) (PUBMED:22498933) (PUBMED:28483520) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_C97