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 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 [].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

Identifier
PF00225
PR00380
PS50067
SM00129
G3DSA:3.40.850.10

0 Found In

4 GO Annotations

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

4 Ontology Annotations

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

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
92509 D8RFB1 PAC:15419137 Selaginella moellendorffii 293  
135318 D8TA26 PAC:15413414 Selaginella moellendorffii 637  
448937 PAC:15409828 Selaginella moellendorffii 1285  
411569 D8RIC6 PAC:15409428 Selaginella moellendorffii 163  
95291 D8RJ59 PAC:15403363 Selaginella moellendorffii 76  
94977 D8RJ58 PAC:15405784 Selaginella moellendorffii 111  
412550 D8RLU8 PAC:15412339 Selaginella moellendorffii 894  
97490 D8RNC4 PAC:15410864 Selaginella moellendorffii 839  
97410 D8RMB3 PAC:15410678 Selaginella moellendorffii 978  
404718 D8QW67 PAC:15412452 Selaginella moellendorffii 175  
438201 PAC:15419509 Selaginella moellendorffii 956  
78149 D8QU83 PAC:15419268 Selaginella moellendorffii 816  
172950 D8RNI8 PAC:15415755 Selaginella moellendorffii 1039  
413179 D8RNL3 PAC:15412253 Selaginella moellendorffii 301  
413860 D8RQG1 PAC:15417571 Selaginella moellendorffii 985  
98850 D8RPX1 PAC:15416703 Selaginella moellendorffii 755  
414001 D8RRB2 PAC:15414298 Selaginella moellendorffii 904  
405204 D8QWK6 PAC:15411524 Selaginella moellendorffii 583  
105868 D8S0R9 PAC:15418017 Selaginella moellendorffii 300  
107634 D8S3M1 PAC:15422140 Selaginella moellendorffii 1300  
109778 D8S6C5 PAC:15406589 Selaginella moellendorffii 660  
81383 D8R093 PAC:15407496 Selaginella moellendorffii 398  
81191 D8QYV9 PAC:15406053 Selaginella moellendorffii 107  
81821 D8QZX7 PAC:15411333 Selaginella moellendorffii 372  
111677 D8S915 PAC:15412014 Selaginella moellendorffii 402  
432536 D8TGB1 PAC:15404239 Selaginella moellendorffii 203  
419840 D8SAQ0 PAC:15412750 Selaginella moellendorffii 241  
113452 D8SC38 PAC:15416291 Selaginella moellendorffii 310  
2601 D8SD37 PAC:15411456 Selaginella moellendorffii 293  
444798 D8SD16 PAC:15419118 Selaginella moellendorffii 616  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            2142876
            8542443
            1832505
            14732151
            15236970
            20587735