Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex (By similarity). Plays a role in chitin deposition in the cell wall, in determination of the budding pattern, and is required for hyphae formation. Localizes to cortical patch-like structures. Enriched at sites of polarized growth, like the growing bud tip, the mother-bud neck after cytokinesis, and the hyphal tip. The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force. The tail domain participates in molecular interactions that specify the role of the motor domain (By similarity). It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding myosin tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3). The IQ domain and the TH1 region are essential for hyphal growth and for endocytosis. The SH3 domain together with the TH3 region are required for the organization of the cortical actin. Phosphorylation of the TEDS site (Ser-366) is required for the polarization of the actin cytoskeleton. Phosphorylation probably activates the myosin-I ATPase activity. Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.