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Bioluminescence is the production and emission of light by the luciferase enzymes in a living organism. The luciferases were identified in different domains of life, but the Lampyridae luciferases are considered for biotechnological and
clinical applications. Recently, the new Iranian luciferase gene from the Lampyroidea maculata has been cloned and characterized. In this study, in silico analysis of this enzyme as the codon usage bias parameters (CAI, CBI, ENC, and rare codons)
were conducted. Furthermore, the 3D structure of this enzyme was modeled in the I-TASSER web server and the status of
these rare codons in this model was studied using SPDBV and PyMOL software. In the following, the substrate-binding site
was studied using the AutoDock Vina. By molecular modeling, some rare codons were identified that may have a critical
role in the structure and function of this enzyme. The GC3% of the CDs was 17/304 and GC3 Skewness was 0.115. The molecular docking analysis recognizes some residues that yield closely related to the DLSA binding site. By these analyses, a
new understanding of the sequence and structure of this enzyme was created, and our findings can be used in some fields of
clinical and industrial biotechnology. This bioinformatics analysis plays an important role in the design of the new recombinant enzyme.
In silico analysis of bacteriophage tail tubular proteins suggests a putative sugar binding site and a catalytic mechanism
