InterPro : IPR012462

Name  Peptidase C78, ubiquitin fold modifier-specific peptidase 1/ 2 Short Name  Peptidase_C78_UfSP1/2
Type  Family 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 [].
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3 Publications

First Author Title Year Journal Volume Pages
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33
Kang SH Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2. 2007 J Biol Chem 282 5256-62
Komatsu M A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier. 2004 EMBO J 23 1977-86



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)