Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG (By similarity). Involved in DNA double-strand break repair (PubMed:30776962). Required for appressorium turgor pressure, autophagy and conidial nuclear degradation (PubMed:30776962). During the germination process and upon starvation conditions, translocates from the nucleus to the cytoplasm where it acetylates ATG3 at 'lys-262' and 'Lys-267', thus influencing autophagy through controlling ATG3-ATG8 interaction (PubMed:30776962). Also acetylates ATG9 at 'Lys-621' to regulate ATG9 binding to vesicles, which is also important for autophagy and pathogenicity (PubMed:30776962). acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein] Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail (By similarity). In the nucleus, interacts with GSK1 and SSB1 (PubMed:30776962). In the cytoplasm, interacts with ATG3 and ATG9 (PubMed:30776962). Is only present in the nucleus under nutrient-rich condition, and translocates from the nucleus to the cytoplasm with the assistance of SSB1 during germination or upon starvation. Phosphorylated at Ser-8 by GSK1 in the nucleus which impairs its translocation to the cytoplasm through interfering the interaction between HAT1 and SSB1. Dephosphorylation under nutrient starvation conditions promotes the interaction between HAT1 and SSB1 and results in the translocation of HAT1 from the nucleus to the cytoplasm in order to acetylate ATG3 and ATG9. Significantly attenuates virulence toward rice leaves by affecting appressorial penetration and infectious hyphal growth (PubMed:30776962). Impairs the acetylation of ATG3 during germination and weakens the interaction between ATG3 and ATG8 (PubMed:30776962). Abolishes also the acetylation of ATG9 and thus impairs the ATG9 binding ability to vesicles during nutrient starvation induction (PubMed:30776962). Belongs to the HAT1 family.