109  structures 183  species 3  interactions 3786  sequences 115  architectures

Family: Kinesin (PF00225)

Summary

Kinesin motor domain Add an annotation

No Pfam abstract.


Literature references

  1. Sablin EP, Kull FJ, Cooke R, Vale RD, Fletterick RJ; , Nature 1996;380:550-555.: Crystal-structure of the motor domain af the kinesin-related motor NCD PUBMED:8606780

  2. Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E; , Cell 1997;91:985-994.: The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. PUBMED:9428521


InterPro entry 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.

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.

Clan

This family is a member of clan AAA (CL0023), which contains the following 142 members:

6PF2K AAA AAA-ATPase_like AAA_2 AAA_3 AAA_5 AAA_PrkA ABC_ATPase ABC_tran Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arch_ATPase Arf ArgK ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 Bac_DnaA CbiA CoaE CobA_CobO_BtuR CobU cobW CPT CTP_synth_N Cytidylate_kin DAP3 DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DnaB_C dNK DUF1253 DUF1611 DUF2075 DUF2478 DUF258 DUF265 DUF699 DUF815 DUF853 DUF87 DUF889 Dynamin_N Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GSPII_E GTP_EFTU Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Herpes_Helicase Herpes_ori_bp Herpes_TK IIGP IPPT IPT IstB KaiC KAP_NTPase Kinesin KTI12 LpxK MCM Mg_chelatase MipZ Miro MMR_HSR1 MobB MutS_V Myosin_head NACHT NB-ARC NOG1 ParA Parvo_NS1 PAXNEB PduV-EutP PhoH Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK Rad17 Rad51 Ras RecA Rep_fac_C ResIII RHD3 RNA12 RNA_helicase RuvB_N SecA_DEAD Septin Sigma54_activat SKI SMC_N SNF2_N Spore_IV_A SRP54 SRPRB Sulfotransfer_1 Sulfotransfer_2 Sulphotransf Terminase_1 Terminase_3 Terminase_6 Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG TrwB_AAD_bind UPF0079 UvrD-helicase Viral_helicase1 VirC1 YhjQ Zeta_toxin Zot

Gene Ontology

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

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HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: kinesin;
Type: Domain
Author: Bateman A, Finn RD
Number in seed: 87
Number in full: 3786
Average length of the domain: 296.60 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 34.51 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.5 22.5
Trusted cut-off 22.5 22.5
Noise cut-off 22.4 22.4
Model length: 333
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 3 interactions for this family. More...

Kinesin Tubulin Tubulin_C

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Kinesin domain has been found.

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