Conidial surface nicotinamide adenine dinucleotide glycohydrolase that cleave NAD(+) and NADP(+) but not their reduced counterparts, NADH and NADPH (PubMed:33712585). Lacks both ADP-ribosyl cyclase and base exchange activity and does not mediate synthesis of calcium messengers cADPR or NAADP (PubMed:33712585). Plays a role in pathogenicity by depleting the host's NAD(+) pool (PubMed:33712585). H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide The catalytic activity is positively regulated by calcium via its binding to the calcium-binding site. Homodimer. Localizes on the surface of conidia. Expression is up-regulated during conidiation of A.fumigatus strains displaying high adherence to pulmonary epithelial cells. The C-terminus contains also a calcium binding site (residues 215-224) that might be involved in NADase activity regulation (PubMed:33712585). The calcium-binding site is not alweays present since it emerged in the order Eurotiales, which includes Aspergillus species (PubMed:33712585). N-glycosylated. Impairs NADase cleavage in conidia. Belongs to the fungal surface NADase family.