| Type: | Family | Name: | Peptidase C78, ubiquitin fold modifier-specific peptidase 1/ 2 |
| Description: | Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad or triad []. This entry contains UfSP1 and UfSP2, which are cysteine peptidases required for the processing and activation of Ubiquitin fold modifier 1 (Ufm1, ) and for its release from conjugated cellular proteins. UfSP1 and UfSP2 are 217 aa and 461 aa respectively [, ]. The peptidases belong to MEROPS peptidase family C78, clan CA. The UfSP2 family have an N-terminal extension with one or more zinc finger domains of the C2H2 type (), which have been shown to be involved in protein:protein interaction. UfSP2 is present in most, if not all, multi-cellular organisms including plants, nematodes, flies, and mammals, whereas UfSP1 is not present in plants and nematodes []. | Short Name: | Peptidase_C78_UfSP1/2 |
