Reliable knowledge on pathogenic agents contributes to effective plant protection. For most plant pathogens, maintaining protein homeostasis (proteostasis) is essential for unfolding the cellular functions to survive and thrive. However, the fungal proteins involved in proteostasis remain poorly characterized in the process of pathogenesis. In this study, we characterized the function of the nascent polypeptide-associated complex (NAC) in Fusarium graminearum (F. graminearum, FgNAC), one of the top 10 fungal pathogens with predominant scientific/economic importance. We found that FgNACα, a subunit of FgNAC, manifests high structural and functional similarity to its homologous counterparts in yeast and other species. The mutants of F. graminearum lacking NACα are viable but suffer significant defects in vegetative growth, conidial production, and pathogenesis. In addition, we show here that FgNACα can interact with another subunit of NAC (FgNACβ) in a yeast-two-hybrid assay. The subcellular localization results show that FgNACα and FgNACβ are predominantly localized in the cytoplasm. Future studies should focus on deciphering the mechanism by which NAC orchestrates protein biogenesis and consequentially modulates development and pathogenesis.