RNA-binding protein that plays a role in the inhibition of multiple cellular antiviral responses activated by double-stranded RNA (dsRNA), such as inhibition of PKR activation, necroptosis, and IFN-mediated antiviral activities (By similarity). Recognizes and binds Z-RNA structures via its Z-binding domain and dsRNA via its DRBM domain: RNA-binding activity is required to escape host ZBP1-dependent necroptosis (By similarity). Mechanistically, the Z-binding domain binds Z-RNAs that are produced during Yaba-like disease virus infection, thereby competing with Z-RNA detection by host ZBP1, suppressing ZBP1-dependent necroptosis (By similarity). The Z-binding domain recognizes and binds Z-nucleic acid structures. Belongs to the poxviridae E3 protein family. Binds Z-DNA structures in vitro (PubMed:15448208). However, it probably binds Z-RNA in vivo (By similarity).