CaMKIV is a monomeric multifunctional serine/threonine protein kinase that is predominantly expressed and has important roles within the nervous and immune system, such as its involvement in the transcription of IL-2 genes within T lymphocytes. Two human isoforms of CaMKIV was also discovered throughout the course of this project, including CaMKIVα and CaMKIVβ, of which we have chosen CaMKIVα to be our representative protein on the basis of it being the most cited protein sequence in most literature studies.

FASTA analysis and multiple sequence alignment of this protein displayed a constellation of CaMKIV from many animal and plant species that exhibit a limited, albeit significant extent of sequence homology when compared to our representative protein (CaMKIVα). The structural domain analysis of CaMKIV indicated four vital domains that are functionally essential for its behaviour within the CaMKIV signalling cascade, and mutations within such domains could result in uncontrolled or abnormal signalling of CaMKIV within its pathway, leading to pathology.

Our BLAST result suggested that specific regions of CaMKIV is evolutionarily conserved amongst many different animals species, with evolutionary more related animals sharing a greater degree of sequence homology than those that are more distant. The BLAST search also implied that CaMKIV may also be a protein that is being intensively studied at the moment, as many predicted (albeit not confirmed) models of this protein exist.