Delving into the unknown has always been a defining quality of humanity. This curiosity extends to even the smallest and most abstract of things, such as viruses. The recent emergence of SARS-CoV2 highlighted the importance of understanding the structures of viral proteins for vaccine design. The pandemic also brought forward as to what could possibly cause the next global health crisis. This project aims to demonstrate the capability of AlphaFold (a protein structure prediction software) in aiding construct design with clear and defined domain boundaries of theoretical proteins. An uncharacterised virus (ThV), where the genetic material and not the virion itself was observed, was studied in this project. Running the viral ORF through AlphaFold yielded intriguing models for an RNA-dependent RNA Polymerase (ThVP) and its viral capsid (ThVC). The resulting models have been used to design the respective constructs for subsequent protein expression. The expression of the different proteins and their assembly state had been validated with Mass Spectroscopy and Mass Photometry, respectively. Using TEM, negative stained samples indicated close resemblance with the predicted models of AlphaFold. In conclusion, this study was able to fully demonstrate the competency of AlphaFold in elucidating the structural intricacies of theoretical proteins derived from an uncharacterised virus (ThV). The findings underscored the value of AlphaFold in improving our understanding of the structural landscape of viruses and potentially enhancing our preparedness for future pandemics.