
-   Protein Accession: P12883
-   Size: amino acids: 1935 amino acids
-   Molecular mass: 223097 Da
-   Domains: P-loop_NTPase, IQ_motif_EF-hand-BS, Myosin_tail, Kinesin_motor_dom_sf, Myosin_head_motor_dom, Myosin_N, Myosin_S1_N, XRCC4-like_C
-   Blocks: IQ calmodulin-binding region, Myosin tail, Myosin N-terminal SH3-like domain
-   Family: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
-   The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils [PMID: 26150528, PMID: 26573747]. Four skip residues (Skip1: Thr-1188, Skip2: Glu-1385, Skip3: Glu-1582 and Skip4: Gly-1807) introduce discontinuities in the coiled-coil heptad repeats. The first three skip residues are structurally comparable and induce a unique local relaxation of the coiled-coil superhelical pitch and the fourth skip residue lies within a highly flexible molecular hinge that is necessary for myosin incorporation in the bare zone of sarcomeres [PMID: 26150528]. Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction.
