ADP-ribosylates double-stranded DNA by targeting the N2 amino group of dG residues; 10-fold less active on tRNA. Induces apoptosis in a range of human cell lines (PubMed:10485873, PubMed:11592983). May play a role in removing unnecessary or harmful cells during pupation (PubMed:15528160) (Probable). May play a role in defense against parasitic wasps; its habitual predator Cotesia glomerata is only susceptible after removal of its eggshell or the surface of the larval caudal vesicle, while other wasps are damaged by this protein (PubMed:23637752) (Probable). The wild-type catalytic domain (residues 1-233) cannot be expressed in E.coli as it is unstable probably due to its toxicity. A catalytic domain fragment (Glu-165 mutated to Gln) binds dsDNA but not ssDNA; the presence of the linker inhibits DNA-binding (PubMed:28765284). a 2'-deoxyguanosine in DNA + NAD(+) = an N(2)-(ADP-L-ribosyl)-2'-deoxyguanosine in DNA + H(+) + nicotinamide Within late stage larvae and pupal stages most protein is found in fat bodies. Highest expression is found in fifth instar larvae, decreasing through prepupae, early-phase pupae (1 day after pupation) and late-phase pupae (at protein level). Much lower levels present in adult. The N-terminus (residues 1-233) has the ADP-ribosylation catalytic domain. NAD(+)-binding or the presence of the linker do not alter the structure of the catalytic domain, however in vitro the presence of the linker masks the DNA- and NAD(+)-binding regions and thus prevents dsDNA-binding by the catalytic domain. Belongs to the pierisin ADP-ribosyltransferase family.