The current Study intends to study the mitochondrial genome proteins specifically focusing on the distribution of intrinsically disordered regions within these proteins. The UniProt were employed to obtain amino acid sequences of the mitochondrial proteins. Next, the obtained sequences were studied to identify their unique features. We used the PONDR VSL2 algorithm to assess the proteins for any order or disorder. According to study results, mitochondrial genome proteins were expected to depict unexpected levels of intrinsic disorder. The results also indicated the possibility of presence of 7 intrinsic disorder regions within these proteins. The disordered regions were mostly found to be associated with protein–protein interactions. The research indicated the presence of two to nine molecular recognition features in the assessed mitochondrial proteins. These features included short structure-prone segments, location of mitochondrial proteins inside long disordered regions and the feature of showing disorder-to-order transition during binding. Moreover, such regions were attributed with a number of sites characterized with posttranslational modifications. According to the analysis, there may be many disordered regions present within mitochondrial genome proteins leading to multifunctional nature of mitochondrial genome proteins in the signal transduction pathways where these proteins regulate the cell metabolism pathways.