Homologous Superfamily

Myosin S1 fragment, N-terminal (IPR008989)

Short name: Myosin_S1_N

Overlapping entries


Myosin is a molecular motor that undergoes ATP-driven conformational changes during force production and motility. The S1 fragment myosin head consists of both the globular motor domain, containing the ATP- and actin-binding sites, and the lever arm, which amplifies small conformational changes in the motor domain into larger motions by which myosin moves actin. The motor domain contains four major subdomains linked by three single-stranded joints: the N-terminal subdomain, the upper 50kDa subdomain, the lower 50kDa subdomain, and the C-terminal converter subdomain [PMID: 11016966]. The N-terminal subdomain has an SH3-like partly opened beta barrel topology, with the last strand being interrupted by a 3-10 helical turn. The N-terminal and upper 50kDa subdomains together form the nucleotide-binding pocket. The binding of specific nucleotides alters the structural state of the myosin head during the contractile cycle.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005524 ATP binding
GO:0051015 actin filament binding
GO:0003774 motor activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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