LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | Members of the myosin superfamily of actin-based motors act in a variety of cellular functions such as muscle contraction, cell and organelle movement,membrane trafficking, and signal transduction. Although myosin motor domains show a high degree of sequence conservation, the individual myosin classes are clearly defined by differences in the head structure. TheN-terminal region of myosins from different classes varies greatly in length and amino acid composition among the individual members. Many myosins have anSH3-like domain at the N terminus of the motor domain. This includes myosins in classes II, V, VI, XI, XXII and XXIV. The myosin N-terminal SH3-like domainmay mediate some aspect of the conformational communication that occurs within the myosin head during actin and nucleotide binding. Part of this effect maybe mediated through interactions with the neck-associated essential light chains that are in close proximity to this portion of the head domain and alsotransiently interact with actin [ , , ].The myosin N-terminal SH3-like domain comprises ~50 amino acids and forms a protruding, six-stranded, antiparallel, β-barrel domainwith similarities to the SH3 domain [ , ]. |
| Short Name | Myosin_N |
