Toxoplasma gondii, an obligate, intracellular, protozoan parasite, is known to infect a wide range of warm-blooded animals, including livestock, marine mammals and humans leading to the development of toxoplasmosis. The dense granule antigens (GRAs) have garnered crucial role in parasite survival, virulence and the formation of the parasitophorous vacuole. The study focusing on the GRA10 protein of T. gondii aims to elucidate its features further to support its potential inclusion in future vaccine formulations. The present study provided an exhaustive elucidation of the key characteristics of the GRA10 protein, encompassing its presence of a transmembrane domain, physico-chemical properties, subcellular localization, potential epitopes recognised by B-cells and T-cells, secondary and tertiary structures, as well as other significant attributes of this protein. The results indicated that the GRA10 protein possesses a total of 192 possible post-translational modification sites, with no transmembrane domains being detected within its structure. In terms of secondary structure, the GRA10 protein is composed of 27.74% alpha-helix, 13.53% extended strand and 58.72% random coil elements. Additionally, various potential B- and T-cell epitopes were pinpointed for the GRA10 protein, suggesting its immunogenic properties. The assessment of antigenicity and allergenicity further confirmed that GRA10 is immunogenic but non-allergenic, making it a promising candidate for further study. Furthermore, the induction of IFN-γ and IL-4 highlighted the ability of related MHC-II molecules to interact with GRA10, indicating its potential role in immune responses. These findings shed light on the multifaceted nature of the GRA10 protein and its significance in immunological processes. The study presented crucial fundamental and theoretical information regarding GRA10 in order to facilitate the creation of a potent vaccine against both acute and chronic toxoplasmosis, warranting additional in vivo examinations.