Vespidae is a cosmopolitan family of order Hymenoptera popularly called as wasps. Hyaluronidase is found in the venom and saliva of stinging insects. Hyaluronidase (HYases) is the major allergen in the venoms of bees, hornets, and scorpions. The Asian hornet Vespa velutina venom protein Hyalouronidase (HYases) sequence was selected for present in-silico analysis. The physicochemical analysis of the predicted Hyaluronidase (HYases) was performed using Protparam tools. The secondary structures of Hyaluronidase were predicted by using SOPMA. The 3D structures were predicted using the SWISS-MODEL server and models were validated. The results show that the most abundant amino acid was found as Asparagine and six type’s motifs were observed and the highest number of the motif was ASN- Glycosylation site and Protein kinase C phosphorylation site. The secondary structure was observed that random coil was predominant (39.88%), followed by alpha helix (39.27%) and extended strand (15.11%). Ramachandran plot analysis showed that residues in most favoured regions is 90.03% residues in additional allowed regions is 9.0% indicating that the model was of reliable and good quality. The results of our study contribute to an understanding of venom protein structure in hornet species and will be scientific base for 3D modeling of Hyalouronidase (HYases) proteins in further studies.