The domain within your query sequence starts at position 190 and ends at position 236; the E-value for the MYSc domain shown below is 6e-12.


The domain was found using the schnipsel database


Myosin. Large ATPases.
SMART accession number:SM00242
Description: ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Interpro abstract (IPR001609):

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, 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) ].

The globular head is well conserved, some highly-conserved regions possibly relating to functional and structural domains [ (PUBMED:6576334) ]. The rod-like tail starts with an invariant proline residue, and contains many repeats of a 28 residue region, interrupted at 4 regularly-spaced points known as skip residues. Although the sequence of the tail is not well conserved, the chemical character is, hydrophobic, charged and skip residues occuring in a highly ordered and repeated fashion [ (PUBMED:6576334) ].

GO component:myosin complex (GO:0016459)
GO function:ATP binding (GO:0005524), motor activity (GO:0003774)
Family alignment:
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There are 33491 MYSc domains in 33449 proteins in SMART's nrdb database.

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