Double-stranded DNA breaks (DSB) are one of the most destructive damages caused by ionizing radiation to cells. Resistance to harsh conditions of ionizing radiation, UV light, and dryness are special characteristics of members of the genus Deinococcus. In order to maintain survival against radiation-induced damage, the bacterium Deinococcus gobensis (strain I-O) has the Rec A protein, which plays a pivotal role in the repair of DSB breaks and recombination. In this study, the three-dimensional structure of the Rec A protein isolated from Deinococcus gobensis strain I-O, which has not been determined experimentally, was simulated by aligning it with the sequence of Deinococcus radiodurans using the Swiss model program. The alignment result showed that the Rec A protein is 80% similar to the human gene. In order to examine the quality of modeling, the Root Mean Square (RMS) was calculated, in the aforementioned model was estimated to be 0.56 angstroms, which was less than 1 and indicated the suitability of the designed model. By predicting and determining three-dimensional structures and modeling proteins, interactions between substrates can be examined and, with the help of bioinformatics, a tool for great success in the field of drug design can be obtained in this field.