Myosin, N-terminal, SH3-like (IPR004009)

Short name: Myosin_N

Overlapping homologous superfamilies

Domain relationships



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. The N-terminal region of myosins from different classes varies greatly in length and amino acid composition among the individual members. Many myosins have an SH3-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 domain may mediate some aspect of the conformational communication that occurs within the myosin head during actin and nucleotide binding. Part of this effect may be mediated through interactions with the neck-associated essential light chains that are in close proximity to this portion of the head domain and also transiently interact with actin [PMID: 16982629, PMID: 17597155, PMID: 20217677].

The myosin N-terminal SH3-like domain comprises ~50 amino acids and forms a protruding, six-stranded, antiparallel, beta-barrel domain with similarities to the SH3 domain [PMID: 16982629, PMID: 15944696].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005524 ATP binding
GO:0003774 motor activity

Cellular Component

GO:0016459 myosin complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles