Structural similarities between the Arabidopsis and coffee NDR1 proteins. Predicted structural domains and motifs of NDR1 proteins are represented. The overall structure of both proteins appears conserved; it is furthermore reminiscent of GPI-anchored proteins . The C-terminus of NDR1 proteins exhibits putative cleavage sites, including the ω-site to which the glycolipid moiety of the anchor is attached. Domains following the attachment site display the necessary features for proper transamidase activity, the enzyme complex involved in GPI modifications of proteins and localized to the ER membrane. A putative uncleavable N-terminal signal peptide that might be implicated in ER targetting is also present in both proteins. TMD indicates a predicted transmembrane domain. The size of each protein domain is indicated as Arabic numbers. The number of predicted glycosylation sites (in the middle domain, shown in light grey) is also indicated above and below the proteins. For convenience, the three conserved NHL motifs are shown as hatched regions I, II and III. Predictive models and methods used for building this scheme are described in the 'Methods' section.