Endosymbiotic theory suggests that plastids originated from a photosynthetic bacterium that was engulfed by a primitive eukaryotic cell. In consequence, the chloroplast genome remains affected by this ancestral event, although it is reduced in size and the number of constituent genes. Most parts of the plastid genome have been transferred to the host cell nuclear genome and are nuclear-encoded. Thus, chloroplast proteins are synthesized in the cytosol as precursors with N-terminal extensions called transit peptides. The evolution of import machinery was required to transfer transit peptides to the stroma. Until the present, two protein complexes have been found to mediate the import process: the Toc (outer) and Tic (inner) envelope membrane translocons. The evolutionary origin of many Tic and Toc proteins has been established, but not for the Tic110 subunit. Tic110 binds signal peptides and serves as a scaffold for the recruitment of stromal components. In this study, we analyzed hydrophobic clusters, protein folds, and protein structure homology and we conclude that Tic110 is composed of fourteen repeated motifs related to HEAT-repeats. The explanation for the presence of such repeats in Tic110 is that membrane arrangement is found in separate domains and their probable function in the chloroplast import process is discussed.