For more than a century, natural oligopeptides have attracted scientific attention as important biochemical regulators. Since that time, thousands natural oligopeptide regulators have been described, and now ~600 new natural oligopeptides emerge annually, out of a literature of >70 000 publications each year on oligopeptide chemistry and biology according to PubMed database. Their primary structure is determined either directly or by translation from nucleotide sequences. Both these ways are experimental and laborous. But there are a lot of unrecognized protein sequences in different public databases which can contain unknown oligopeptide structures. Thereupon we have carried out a theoretical structure–function analysis of known uncharacterized protein amino acid residue sequences in order to identify new oligopeptide primary structures. As an example, grape (Vitis vinifera) proteins were chosen. A special computer analysis was developed for such analysis. The data of GenBank and SwissProt databases containing primary structures of unrecognized grape proteins, EROP-Moscow database containing information on structure and functions of plant regulatory oligopeptides and specially created computer programs for the comparison of GenBank or SwissProt information with EROP-Moscow data were used. This method permitted to reveal new potentially active regulatory oligopeptide sequences after alignment procedure. It was been found 21 grape protein structure sites homologues to known regulatory oligopeptides elucidated from other plant species. Their similarity with other plant oligopeptide primary structures was from 54.4 to 95.7%. They can be characterized as putative antimicrobial oligopeptides and rapid alkalinization factors. The problem of existence of these oligopeptide structures in grape is discussed. It has been proposed that rapid alkalinization factors can also possess antimicrobial activity. This way of oligopeptide structure elucidation can be extended to oligopeptide structures of any functional class.FONDECYT149FONDECYT