The domain within your query sequence starts at position 799 and ends at position 1144; the E-value for the Myosin_tail_1 domain shown below is 2.2e-37.



PFAM accession number:PF01576
Interpro abstract (IPR002928):

Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains [ (PUBMED:1939027) ], 2 alkali light chains, and 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C-terminal coiled-coil rod-like tail [ (PUBMED:11919279) ], although some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains, coded for by a multi-gene family [ (PUBMED:2806546) ]. Myosin interacts with actin to convert chemical energy, in the form of ATP, to mechanical energy [ (PUBMED:3540939) ]. The 3-D structure of the head portion of myosin has been determined [ (PUBMED:8316857) ] and a model for actin-myosin complex has been constructed [ (PUBMED:8316858) ].

This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament [ (PUBMED:3783701) ]. The coiled-coil region provides the structural backbone of the thick filament [ (PUBMED:3783701) ].

GO component:myosin complex (GO:0016459)
GO function:motor activity (GO:0003774)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Myosin_tail_1