The domain within your query sequence starts at position 136 and ends at position 287; the E-value for the KISc domain shown below is 2e-36.


The domain was found using the schnipsel database


Kinesin 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 comprises five motifs, namely N1 (P-loop), N2 (Switch I), N3 (Switch II), N4 and L2 (KVD finger) [ (PUBMED:20587735) ]. It has a mixed eight stranded beta-sheet core with flanking solvent exposed alpha-helices and a small three-stranded antiparallel beta-sheet in the N-terminal region [ (PUBMED:15236970) ].

A number of proteins have been recently found that contain a domain similar to that of the kinesin 'motor' domain [ (PUBMED:8542443) (PUBMED:1832505) ]:

  • Drosophila melanogaster claret segregational protein (ncd). Ncd is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The ncd motor activity is directed toward the microtubule's minus end.
  • Homo sapiens CENP-E [ (PUBMED:1832505) ]. CENP-E is a protein that associates with kinetochores during chromosome congression, relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division. CENP-E is probably an important motor molecule in chromosome movement and/or spindle elongation.
  • H. sapiens mitotic kinesin-like protein-1 (MKLP-1), a motor protein whose activity is directed toward the microtubule's plus end.
  • Saccharomyces cerevisiae KAR3 protein, which is essential for nuclear fusion during mating. KAR3 may mediate microtubule sliding during nuclear fusion and possibly mitosis.
  • S. cerevisiae CIN8 and KIP1 proteins which are required for the assembly of the mitotic spindle. Both proteins seem to interact with spindle microtubules to produce an outwardly directed force acting upon the poles.
  • Emericella nidulans (Aspergillus nidulans) bimC, which plays an important role in nuclear division.
  • A. nidulans klpA.
  • Caenorhabditis elegans unc-104, which may be required for the transport of substances needed for neuronal cell differentiation.
  • C. elegans osm-3.
  • Xenopus laevis Eg5, which may be involved in mitosis.
  • Arabidopsis thaliana KatA, KatB and katC.
  • Chlamydomonas reinhardtii FLA10/KHP1 and KLP1. Both proteins seem to play a role in the rotation or twisting of the microtubules of the flagella.
  • C. elegans hypothetical protein T09A5.2.

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 function:microtubule motor activity (GO:0003777), microtubule binding (GO:0008017), ATP binding (GO:0005524)
Family alignment:
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There are 50033 KISc domains in 50005 proteins in SMART's nrdb database.

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