author(s)
Rumpi Ghosh, AD Upadhyay, AK Roy and Ajit Tiwari

abstract
The aquaporin (AQP) developed the most conserved class of protein families and plays a lead role in water transport and conservation in fish organ. This research was conducted basically focused on structural and functional analysis of aquaporin protein of 10 different fish sequence with Protparam, CFSSP, PSIPRED, SOPMA, Swiss model, Phyre2 etc. Through the physicochemical analysis it was proved that protein is unstable, quietly thermostable and Gravy of this protein shows hydrophilic property. And helix percentage range between 50.5-81.4%, sheets range 40.6-78 and turn range 7-15. Alpha helix and beta sheets are connected through the turns. Turns play a key role in folding by bringing together interactions between regular secondary structure elements. A turn helps to stabilize abrupt directional changes in the polypeptide chain. The tertiary structure of aquaporin in different fish was predicted by Swiss model, Phyre 2 and TM score servers and their similarity was verified by Verified 3D and ramachandran plot. For tertiary structure prediction ‘1j4n’ (Bos taurus) was select as a model template. Phylogenetic tree was structured or constructed by MEGA 7 tools by neighbour joining method. According to the results, they derived from common ancestors. Protein-protein interaction was performed by String. After verification we get an Accession number through the PMDB. This obtained data provided a background for bioinformatics studies of structure and function also evolution of other organism.