Table demonstrates that the tau protein possesses RNase activity, and RNase III activity is nearly ubiquitous throughout the sequence. It looks like the tau protein can find the double-stranded guide RNA of the telomeric fragment and the target DNA sequence. It can then cut the guide RNA of the telomeric fragment. By the Exosome-associated factor Rrp6 N-terminal and Exoribonuclease phosphorolytic domain of tau protein, the cut guide RNA is transported to the exosome for its degradation. active site residues create a magnesium catalytic center, which cleaves the 3' overhang in a time-dependent manner, forming a typical RNase fold. It bears a striking resemblance to a DEDD-type RNase, a unique ATP-binding protein that binds both ATP and dATP. It dimerizes and bonds magnesium ions through Asp-6.