The precise mechanisms underlying the profound influence of aberrant tau protein phosphorylation and aggregation on Alzheimer's disease remain elusive. This study used bioinformatics methods, specifically protein domain search tools, to look into how the tau protein causes neurodegenerative diseases. The study demonstrates that the tau protein has domains associated with the Aging Device. The domain list includes pyruvate kinase, phosphatase, telomere binding, telomere transposition, HNH cas9, replicon binding, helicase, DNA polymerase, nuclease, transcription factors-like, promoter binding (TATA-box), enhancer binding (Homeobox, MADS-box, HMG box), and mitochondrial localization. It suggests that the pyruvate kinase domain of the tau protein provides ATP energy for its Aging Device activity. After the HNH Cas9, reverse transcriptase, and transposase domains cut the DNA sequence between the "TAA" region of the telomere, then transcript the guide RNA sequence. The transcription factor domain moves to the exact location on the DNA where it binds. The HNH Cas9 domain removes the intron DNA region that is complementary to the guide RNA sequence. The nuclease and transposase domains splice the "TAA" region from the promoter or enhancer and add the telomere fragment sequence. We thought that tau protein could interface with the function of RNA polymerase II by moving telomere fragments to the promoter/enhancer area. This would make the Aging Device's telomere-guided gene (DNA in the nucleus or mitochondrial ) copy number decrement regulatory system work better. Stress injuries, such as low blood sugar or oxygen levels, can lead to tau protein aggregation and phosphorylation, resulting in a perplexing deactivation of the Aging Device. Therefore, neurodegenerative disorders like Alzheimer disease, amyotrophic lateral sclerosis may potentially link to the atypical functioning of aging devices like tau protein.