Translation elongation factor-1alpha (EF-1α) or its paralog elongation factor-like proteins (EFL) interact with an aminoacyl-transfer RNA (aa-tRNA) to play its essential role in elongation of peptide-chain during protein synthesis. Species usually have either an EF-1α or EFL protein; however, some species have both EF-1α and EFL (dual-EF-containing species). In the dual-EF-containing species, EF-1α appeared to be highly divergent in the sequence. Homology modeling and surface analysis of EF-1α and EFL were performed to examine the hypothesis that the divergent EF-1α in the dual-EF-containing eukaryotes does not strongly interact with aa-tRNA compared to the canonical EF-1α and EFL. The subsequent molecular dynamics simulations were carried out to confirm the validity of modeled structures and to analyze their stability. It was found that the molecular surfaces of the divergent EF-1α proteins were negatively charged partly, and thus they might not interact with negatively charged aa-tRNA as strongly as the canonical ones. The molecular docking simulations between EF-1α/EFL and aa-tRNA also support the hypothesis.