KIScKinesin motor, catalytic domain. ATPase.
|SMART accession number:||SM00129|
|Description:||Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.|
|Interpro abstract (IPR001752):|
Kinesin [(PUBMED:8542443), (PUBMED:2142876), (PUBMED:14732151)] is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.
The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyse ATP, to bind and move on microtubules), a central alpha-helical coiled coil domain that mediates the heavy chain dimerisation; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.
The kinesin motor domain is located in the N-terminal part of most of the above proteins, with the exception of KAR3, klpA, and ncd where it is located in the C-terminal section.
The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90, the C-terminal half of the domain is involved in microtubule-binding.
|GO process:||microtubule-based movement (GO:0007018)|
|GO component:||microtubule associated complex (GO:0005875)|
|GO function:||microtubule motor activity (GO:0003777), ATP binding (GO:0005524)|
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