Deciphering the origin of eukaryotes is an unresolved question that has been obscured by several controversies over the past decades. In recent years, phylogenomic analysis of environmentally sampled DNA revealed the existence of eukaryotic features in the genome of a group of organisms belonging to the archaeal clade known as “Asgard”. This study seeks to investigate the structural relationship between the components of Asgard oligosaccharyltransferase (OST) complex (also known as N-glycosylation complex) and that of their eukaryotic counterparts. We solved the X-ray structure of the C-terminal domain of ribophorin I from Prometheoarchaeum syntrophicum’ strain, MK-D1. This domain shares a four-helical bundle fold with the equivalent domain from human ribophorin I. We used AlphaFold2 to predict a model of the enzymatic subunit, staurosporine and temperature-sensitive (STT3) from the putative Asgard OST complex. This model shares high structural similarity with the eukaryotic counterpart, namely the STT3A isoform. Furthermore, structure-based comparison between the AlphaFold2 model of Asgard SecY and the X-ray structure of human Sec61α highlights the evolutionary relationship between Asgard archaea and eukaryotes. Studies are underway to uncover the functional relationships among MK-D1 OST proteins and eukaryotes. Although spaced by several years of evolutionary innovation, the existence of prominent eukaryotic-like OST features in Asgard genomes supports the growing evidence for an “Asgard-eukaryote” evolutionary transition.