We have also used Iterative Threading ASSEmbly Refinement (I-TASSER) to determine the protein’s structure and predicted biological function (4, 5, 6). An amino acid sequence is submitted and the programme detects known proteins in the PDB that have similar folds to the protein (but without using close homologous proteins) in question to create a ‘best fit’. It then aligns the target sequence with the proteins from the database and then the folds are assembled to create the most probable three dimensional protein model. Finally, the sequence is annotated the structural domains and their functions. I-TASSER predicted 5 final models whose C-score (on a scale between -5 to 2) ranged between -3.18 to 2.85 which is relatively low, which indicates the quality of the predicted models. We have only included the first model out of the five generated. The eEF2K protein was predicted to consist of 34.6% helical, 9.5% beta strands and 55.9% coiled structures.