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¹ University of Rajshahi, Faculty of Life and Earth Science, Department of Genetic Engineering & Biotechnology, Rajshahi-6205, Bangladesh
² Jashore University of Science and Technology, Faculty of Biological Science, Department of Fisheries and Marine Bioscience, Jashore-7408, Bangladesh
³ Chulalongkorn University, Faculty of Veterinary Science and Technology, Department of Veterinary Microbiology, Bangkok-10330, Thailand DOI : 10.4194/AFS37 - Unknown or hypothetical proteins exist, but they have yet to be identified or correlated to gene sequences. Domains of unknown function are proteins that have been identified experimentally but do not have a known functional or structural domain. Using a variety of computational approaches and tools, this research investigated and characterized the likely functional characteristics of a hypothetical protein from Vibrio parahaemolyticus (Accession no. QOS18375.1). The physicochemical characteristics, subcellular localization, three-dimensional structure, protein-protein interactions, and functional elucidation of the protein are all available from this in silico perspective. Protein-protein interactions are investigated using the STRING software and resulted that VP128 putative protein interacts strongly with the GlpX type protein Fructose-1,6-bisphosphatase. The in-silico investigation documented the protein`s hydrophilic nature with predominantly alpha (α) helices in its secondary structure. Furthermore, the protein, according to the research, features a VP128 domain and is thought to bind ribosomal subunits and the top active sites of the model described also. Therefore, the research findings will facilitate the development of new antibacterial drugs against acute gastroenteritis and other serious diseases by providing a better knowledge of the role of VP128 domain. Keywords : Vibrio parahaemolyticus, Hypothetical protein, Characterization, Homology, CASTp