Protein Domain : Legumain prodomain superfamily IPR046427

Type	Homologous_superfamily
Description	Asparaginyl endopeptidase, also known as legumain, is a family of cysteine proteases found in many organisms. This group of cysteine peptidases belong to the MEROPS peptidase family C13 (legumain family, clan CD). A type example is legumain from Canavalia ensiformis (Jack bean, Horse bean) [ ]. Although legumains were first described from beans (also known as Vacuolar Processing Enzymes), homologues have been identified in plants, protozoa, vertebrates, and helminths [, ]. In blood-feeding helminths, asparaginyl endopeptidases (sometimes described as hemoglobinases) have been located in the gut and are considered to be involved in host hemoglobin digestion [, , , ].This domain is found in the proenzyme form legumain (also known of Vacuolar-processing enzyme). The mature active form of these proteins is generated by autoproteolytic maturation at acidic pH. In the 3D structure of the proenzyme, this prodomain is located on top of the protease domain, blocking access to the active site, conferring enzymatic latency and conformational stability. It shows an entirely α-helical fold, with an activation peptide and a region that assemblies into a death domain-like fold at the C-terminal (also referred to as as legumain stabilization and activity modulation (LSAM) domain) [].
Short Name	Legumain_prodom_sf