Forecasting the three-dimensional configuration of a particular protein is challenging due to the vast array of possible conformations that the amino acid sequence could adopt ( ). However, AlphaFold ( ) initiates its computational exploration for the probable structure by utilising a template, a pre-existing structure for similar proteins. Alternatively, AlphaFold can utilise data on the biological evolution of amino-acid sequences within the protein family, which consists of proteins with similar activities and presumably possess identical folds ( ). The information used in AlphaFold is valuable because consistent associated evolutionary changes in pairs of amino acids suggest that these amino acids have a direct interaction despite being located far apart in the sequence ( ). Information of this nature can be derived from protein families' multiple sequence alignments (MSAs), obtained by analysing the evolutionary differences in sequences across different biological species. Nevertheless, the dependence on MSAs is limiting due to the unavailability of evolutionary knowledge for all proteins ( ). 13