The domain within your query sequence starts at position 37 and ends at position 78; the E-value for the Myosin_N domain shown below is 3.8e-17.



PFAM accession number:PF02736
Interpro abstract (IPR004009):

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 [ (PUBMED:16982629) (PUBMED:17597155) (PUBMED: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 [ (PUBMED:16982629) (PUBMED:15944696) ].

GO component:myosin complex (GO:0016459)
GO function:ATP binding (GO:0005524), motor activity (GO:0003774)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Myosin_N