Importantly, 1,2fucosyltransferase transferase is present in A. deanei but not in the S. culicis dataset, and fucose residues were found in high amounts on glycoinositolphospholipid molecules of A. deanei, different from the observations for other trypanosomatids. Although the role of fucose is unknown, 
fucose and arabinose Albaspidin-AA transfer to lipophosphoglycan of Leishmania is noticed when the culture medium is supplemented with this carbohydrate, suggesting that fucose might have a specific role in A. deanei-insect interactions. Another glycosyltransferase found in both A. deanei and S. culicis genomes and involved in the N-glycosylation of asparagine residues is the dolichyl-diphosphooligosaccharide-protein glycosyltransferase, an oligosaccharyltransferase that is not classified in any of the above-mentioned families. The A. deanei and S. culicis DDOSTs contain the STT3 domain, a subunit required to establish the activity of the oligosaccharyl transferase complex of proteins, and they are orthologous to the human DDOST. These OTase complexes are responsible for transferring lipid-linked oligosaccharides to the asparagine side chain of the acceptor polypeptides in the endoplasmic reticulum, suggesting a conserved N-glycosylation among the trypanosomatids. Five different GalfT sequences are also present in the endosymbiont-bearing trypanosomatids, and all of them contain the proposed catalytic site, indicating genetic redundancy. Redundancy of GalfTs is commonly observed in many different trypanosomatid species, as different transferases are used for each linkage type. As b-galactofuranose has been shown to participate in trypanosome-host interactions, their presence in A. deanei and S. culicis might also indicate a role in the interaction with the insect host. However, no enzymes involved in synthesis of b-Galf-containing glycoconjugates are detected in our A. deanei dataset, despite reports of enzymes involved in b-Galf synthesis in Crithidia spp.. The presence of the N-terminal fatty acid acylation motif was found in some members of calpain-like cysteine peptidases, indicating that some of these peptidases are associated with membranes, as has also been shown for other members of the family. The relatively large amount of calpain-like peptidases may be related to the presence of the endosymbiont, which would require a more complex regulation of the cell cycle and intracellular organelle distribution, as cytosolic calpains were found to regulate cytoskeletal remodeling, signal transduction, and cell differentiation. A second large gene family in the A. deanei and S. culicis genomes encoding 3,4,5-Trimethoxyphenylacetic acid surface proteins with proteolytic activity is gp63. In our genomic analyses, we identified 37 and 9 genes containing sequences homologous to the gp63 of Leishmania and Trypanosoma spp. in the genomes of A. deanei and S. culicis, respectively. Proteins belonging to this group of zinc metalloproteases, also known as major surface protease or leishmanolysin, have been characterized in various species of Leishmania and Trypanosoma. Extensive studies on the role of this family in Leishmania indicate that they are involved in several aspects of host-parasite interaction including resistance to complement-mediated lysis, cell attachment, entry, and survival in macrophages.