The mhcA gene from the human pathogen Entamoeba histolytica was identified using the polymerase chain reaction. It is a single copy gene expressed as a 6.4-kb mRNA. The deduced MhcA protein sequence is highly similar to myosin II from both Dictyostelium discoideum and Acanthamoeba castellanii. The globular head domain of MhcA contains the specific regions involved in ATP binding, actin binding, and interaction with myosin light chain. The tail domain is organized in an alpha-helical coiled coil structure, which suggests that MhcA is an alpha-fibrous protein. The coiled coil is interrupted by two prolines indicating that like other myosins, either from smooth muscle or from non-muscle cells, the tail of MhcA folds twice on itself. In addition, MhcA presents sequence similarities with the heavy chain phosphorylation sites of smooth and non-muscle vertebrate myosins.