CASTp 3.0 predicted 52 amino acids to be involved in the potent active sites (Fig. ). The best active site was found in areas with 968.799 and a volume of 3258.076 amino acids (Fig. ). Chain A contains 32 active sites with 15 different amino acids (R, S, G, M, A, Y, Q, I, V, T, K, P, C, F, D) and chain B contains 20 active sites with 14 different amino acids (N, R, S, Q, I, K, P, C, G, F, T, L, D, M). Determined active sites would be helpful for further analysis during the study of pathogenesis, drug and vaccine development. ScanProsite and Motif also showed the presence of tricopeptide repeat domain and rubredoxin metalbinding domain. Rubredoxin helps to form small non-heme iron-binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. The main feature of this domain is the extended loop or knuckles. Rubredoxin domain binds intimately with tricopeptide motif and this association is essential for lipopolysaccharide regulation and growth into bacterial cells . Lipopolysaccharide at the outer membrane of the cell wall contributes significantly to the pathogenicity of Y. pestis as it enables the bacterium with unique ability to overcome the defense mechanism of both mammalian and insect hosts as well as antibiotics by using lipid A as an anchor to keep the LPS bounded to the membrane whereas orienting its carbohydrate chain towards the environment . After amino acid composition based analysis, VirulentPred suggested this protein as virulent. The globin-like folding pattern was predicted by PFP-FunDSeqE. InterPro server predicted TPR (tricopeptide repeat)-like superfamily for the hypothetical protein. All these results confirm the role of the protein in the metabolic process of lipopolysaccharides, a group of related, structurally complex components of the outer membrane of gram-negative bacteria.