Since the great split between flora and fauna, which based on fossil records occurred around 400 million years ago, ancestral genes and the proteins they encode have differentiated significantly with respect to their sequence ? often beyond a recognition limit. However, in some cases, similarities in folding topology may reveal proteins with a common lineage and ultimately infer a functional similarity. This relationship can help to fully comprehend a lesser-known protein based on its family?s properties. Research shows a sound possibility of such a monophyletic relationship between phytocyanins and ephrins based on recently documented strong similarities in their respective structures. We conducted studies to prove that such a relationship exists. The DNA sequence encoding ephrin proteins was obtained and then mutated to coordinate with the copper binding site in blue copper proteins. This DNA will be expressed in bacterial and yeast vectors. In addition, precursor DNA from mouse ephrin A1, mouse ephrin B1, cucumber stellacyanin and arabidopsis early nodulin were expressed in E.coli to investigate the effect on the growth of the cells and a possible relationship between all proteins.