Fig. 1. Schematic representation of the predicted NMY-1 structure. The N terminus contains an SH3-like domain and a myosin motor domain, which contains the MLC binding sites (one for the regulatory MLC and one for the essential MLC). The C terminus includes a coiled-coil myosin tail domain, probably involved in MHC dimerization. nmy-1 mutations are indicated. The overall amino acid identities between NMY-1 and Drosophila Zipper, human MHCB and C. elegans NMY-2 are shown as well as the identities between the SH3, myosin motor and myosin tail domains.