Deinococcus radiodurans, an extremophile bacterium renowned for its exceptional resistance to radiation, serves as a model organism for studying DNA repair mechanisms. This study focuses on the hypothetical protein DR_0423 (accession AAF10011) from D. radiodurans, aiming to elucidate its structural and functional characteristics through bioinformatics analysis. The sequence of DR_0423 was retrieved and analyzed using BLASTp, revealing significant homology with single-stranded DNA-binding proteins, particularly DdrA proteins involved in DNA damage response. Multiple sequence alignment and phylogenetic analysis confirmed its close relationship with DNA repair proteins across different Deinococcus species. Physicochemical analysis indicated a cytoplasmic localization with a molecular weight of 23,002.15 Da and a theoretical pI of 6.17, suggesting stability under varying conditions. Secondary structure predictions showed a mix of alpha helices, beta strands, and random coils, while 3D modeling based on homologous templates (e.g., Rad52 protein). Validation of the model using PROCHECK and other quality assessment tools confirmed its reliability, and CASTp analysis identified a key active site involved in DNA binding. The findings highlight DR_0423’s potential role in DNA repair, reinforcing the importance of further experimental studies to validate these computational predictions and explore its applications in biotechnology and bacterial genetics.
