Protein Domain : IPR001752

Type:  Domain Name:  Kinesin motor domain
Description:  Kinesin [, , ]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) []. It has amixed eight stranded beta-sheet core with flanking solvent exposed alpha-helices and a small three-stranded antiparallel beta-sheet in the N-terminal region [].A number of proteins have been recently found that contain a domain similar to that of the kinesin 'motor' domain [, ]:Drosophila melanogasterclaret 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 sapiensCENP-E []. 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 cerevisiaeKAR3 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 elegansunc-104, which may be required for the transport of substances needed for neuronal cell differentiation.C. elegans osm-3.Xenopus laevisEg5, which may be involved in mitosis.Arabidopsis thalianaKatA, KatB and katC.Chlamydomonas reinhardtiiFLA10/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. Short Name:  Kinesin_motor_dom

0 Child Features

1 Contains

DB identifier Type Name
IPR019821 Conserved_site Kinesin motor domain, conserved site

5 Cross Referencess


0 Found In

4 GO Annotations

GO Term Gene Name Organism
GO:0003777 IPR001752
GO:0005524 IPR001752
GO:0008017 IPR001752
GO:0007018 IPR001752

0 Parent Features

12564 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
111677 D8S915 PAC:15412014 Selaginella moellendorffii 402  
118774 D8SK89 PAC:15410976 Selaginella moellendorffii 595  
121544 D8SNT0 PAC:15418391 Selaginella moellendorffii 91  
125786 D8SVD8 PAC:15409375 Selaginella moellendorffii 388  
126650 D8SWQ5 PAC:15411496 Selaginella moellendorffii 869  
2601 D8SD37 PAC:15411456 Selaginella moellendorffii 293  
409859 PAC:15405509 Selaginella moellendorffii 1224  
411569 D8RIC6 PAC:15409428 Selaginella moellendorffii 163  
445286 D8SHE5 PAC:15418131 Selaginella moellendorffii 962  
77487 D8QTM8 PAC:15418754 Selaginella moellendorffii 112  
81383 D8R093 PAC:15407496 Selaginella moellendorffii 398  
84640 D8R4C5 PAC:15418597 Selaginella moellendorffii 844  
88228 D8RAA0 PAC:15404746 Selaginella moellendorffii 399  
91328 D8RET9 PAC:15414774 Selaginella moellendorffii 330  
94977 D8RJ58 PAC:15405784 Selaginella moellendorffii 111  
97490 D8RNC4 PAC:15410864 Selaginella moellendorffii 839  
135318 D8TA26 PAC:15413414 Selaginella moellendorffii 637  
172950 D8RNI8 PAC:15415755 Selaginella moellendorffii 1039  
180753 D8SLE5 PAC:15415595 Selaginella moellendorffii 1133  
3347 D8RBC0 PAC:15412148 Selaginella moellendorffii 320  
402396 D8QQH7 PAC:15403580 Selaginella moellendorffii 748  
234668 D8SNV7 PAC:15404671 Selaginella moellendorffii 632  
404718 D8QW67 PAC:15412452 Selaginella moellendorffii 175  
410457 D8RET7 PAC:15405652 Selaginella moellendorffii 163  
444798 D8SD16 PAC:15419118 Selaginella moellendorffii 616  
4729 D8QTM7 PAC:15418062 Selaginella moellendorffii 176  
448937 PAC:15409828 Selaginella moellendorffii 1285  
61072 D8RD87 PAC:15413287 Selaginella moellendorffii 771  
767 D8QNF5 PAC:15422278 Selaginella moellendorffii 656  
77321 D8QRQ9 PAC:15417804 Selaginella moellendorffii 322  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID