Peptidase M35 domain of Asp f2, a major allergen from Aspergillus fumigatus, and related proteins; non catalytic
In this domain subgroup the unique zinc-binding motif (the aspzincin motif, characteristic of the M35 deuterolysin family, and defined as the "HEXXH + D" motif: two His ligands and Asp as third ligand), is poorly conserved and may not bind Zinc. Members of this subgroup also lack a key conserved Tyr residue which acts as a proton donor during metallopeptidase catalysis. These include Asp f2, a major allergen from Aspergillus fumigatus, which reacts with serum from patients with ABPA (allergic bronchopulmonary aspergillosis), and pH-regulated antigen 1 (PRA1) from Candida albicans, which has a role in fungal morphogenesis and perhaps in the host-parasite interaction during candidal infection. No protease activity has been detected for Asp f2 to date. This subgroup also includes Saccharomyces cerevisiae Zps1p. The expression of the Zsp1 gene is increased in response to zinc deficiency; it is a target of the Zap1p transcription factor.
Feature 1:putative Zn binding site [ion binding site]
Evidence:
Comment:In this domain subgroup the unique zinc-binding motif (the aspzincin motif, characteristic of the M35 deuterolysin family (defined as the "HEXXH + D" motif: two His ligands and Asp as third ligand), is poorly conserved and may not bind Zinc. It also lacks a key conserved Tyr residue which acts as a proton donor during metallopeptidase catalysis.
Jiyao W et al.(2023). "The conserved domain database in 2023.",