The filamentous fungus Aspergillus nidulans primarily reproduces by forming asexual spores called conidia, the integrity of which is governed by the NF-kappa B type velvet regulators VosA and VelB. The VosA-VelB hetero-complex regulates the expression of spore-specific structural and regulatory genes during conidiogenesis. Here, we characterize one of the VosA/VelB-activated developmental genes, called vadA, the expression of which in conidia requires activity of both VosA and VelB. VadA (AN5709) is predicted to be a 532-amino acid length fungal-specific protein with a highly conserved domain of unknown function (DUF) at the N-terminus. This DUF was found to be conserved in many Ascomycota and some Glomeromycota species, suggesting a potential evolutionarily conserved function of this domain in fungi. Deletion studies of vadA indicate that VadA is required for proper downregulation of brlA, fksA, and rodA, and for proper expression of tpsA and orlA during sporogenesis. Moreover, vadA null mutant conidia exhibit decreased trehalose content, but increased beta(1,3)-glucan levels, lower viability, and reduced tolerance to oxidative stress. We further demonstrate that the vadA null mutant shows increased production of the mycotoxin sterigmatocystin. In summary, VadA is a dual-function novel regulator that controls development and secondary metabolism, and participates in bridging differentiation and viability of newly formed conidia in A. nidulans.