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149  structures 436  species 3  interactions 9740  sequences 241  architectures

Family: Kinesin (PF00225)

Summary: Kinesin motor domain

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This is the Wikipedia entry entitled "Kinesin". More...

Kinesin Edit Wikipedia article

Animation of kinesin walking on a microtubule
The kinesin dimer attaches to, and moves along, microtubules.
Diagram illustrating motility of kinesin.

A kinesin is a protein belonging to a class of motor proteins found in eukaryotic cells. Kinesins move along microtubule filaments, and are powered by the hydrolysis of ATP (thus kinesins are ATPases). The active movement of kinesins supports several cellular functions including mitosis, meiosis and transport of cellular cargo, such as in axonal transport. Most kinesins walk towards the plus end of a microtubule, which, in most cells, entails transporting cargo from the centre of the cell towards the periphery. This form of transport is known as anterograde transport. In contrast, dyneins are motor proteins that move toward the microtubules' minus end.

The Kinesins

Kinesins were discovered as microtubule (MT)-based anterograde intracellular transport motors.[1] The founding member of this superfamily, kinesin-1, was isolated as a heterotetrameric fast axonal organelle transport motor consisting of 2 identical motor subunits (KHC) and 2 "light chains" (KLC) via microtubule affinity purification from neuronal cell extracts.[2] Subsequently a different, heterotrimeric plus-end-directed MT-based motor named kinesin-2, consisting of 2 distinct KHC-related motor subunits and an accessory "KAP" subunit, was purified from echinoderm egg/embryo extracts[3] and is best known for its role in transporting protein complexes (IFT particles) along axonemes during cilium biogenesis.[4] Molecular genetic and genomic approaches have led to the recognition that the kinesins form a diverse superfamily of motors that are responsible for multiple intracellular motility events in eukaryotic cells.[5][6][7][8] For example, the genomes of mammals encode more than 40 kinesin proteins,[9] organized into at least 14 families named kinesin-1 through kinesin-14.[10]

Structure

Overall structure

Members of the kinesin superfamily vary in shape but the prototypical kinesin-1 is a heterotetramer whose motor subunits (heavy chains or KHCs) form a protein dimer (molecule pair) that binds two light chains (KLCs).

The heavy chain of kinesin-1 comprises a globular head (the motor domain) at the amino terminal end connected via a short, flexible neck linker to the stalk – a long, central alpha-helical coiled-coil domain – that ends in a carboxy terminal tail domain which associates with the light-chains. The stalks of two KHCs intertwine to form a coiled-coil that directs dimerization of the two KHCs. In most cases transported cargo binds to the kinesin light chains, at the TPR motif sequence of the KLC, but in some cases cargo binds to the C-terminal domains of the heavy chains.[11]

Kinesin motor domain

Kinesin motor domain
Kinesin motor domain 1BG2.png
Crystallographic structure of the human kinesin motor domain depicted as a rainbow colored cartoon (N-terminus = blue, C-terminus = red) complexed with ADP (stick diagram, carbon = white, oxygen = red, nitrogen = blue, phosphorus = orange) and a magnesium ion (grey sphere).[12]
Identifiers
Symbol Kinesin motor domain
Pfam PF00225
InterPro IPR001752
SMART SM00129
PROSITE PS50067
SCOP 1bg2
SUPERFAMILY 1bg2
CDD cd00106

The head is the signature of kinesin and its amino acid sequence is well conserved among various kinesins. Each head has two separate binding sites: one for the microtubule and the other for ATP. ATP binding and hydrolysis as well as ADP release, change the conformation of the microtubule-binding domains and the orientation of the neck linker with respect to the head; this results in the motion of the kinesin. Several structural elements in the Head, including a central beta-sheet domain and the Switch I and II domains, have been implicated as mediating the interactions between the two binding sites and the neck domain. Kinesins are related structurally to G proteins, which hydrolyze GTP instead of ATP. Several structural elements are shared between the two families, notably the Switch I and Switch II domains.

Cargo transport

In the cell, small molecules such as gases and glucose diffuse to where they are needed. Large molecules synthesised in the cell body, intracellular components such as vesicles, and organelles such as mitochondria are too large (and the cytosol too crowded) to diffuse to their destinations. Motor proteins fulfill the role of transporting large cargo about the cell to their required destinations. Kinesins are motor proteins that transport such cargo by walking unidirectionally along microtubule tracks hydrolysing one molecule of adenosine triphosphate (ATP) at each step.[13] It was thought that ATP hydrolysis powered each step, the energy released propelling the head forwards to the next binding site.[14] However, it has been proposed that the head diffuses forward and the force of binding to the microtubule is what pulls the cargo along.[15]

There is significant evidence that cargoes in-vivo are transported by multiple motors.[16][17][18][19]

Direction of motion

Motor proteins travel in a specific direction along a microtubule. This is because the microtubule is polar and the heads only bind to the microtubule in one orientation, while ATP binding gives each step its direction through a process known as neck linker zippering.[20]

Most kinesins walk towards the plus end of a microtubule which, in most cells, entails transporting cargo from the centre of the cell towards the periphery. This form of transport is known as anterograde transport/orthrograde transport. Kinesin-14 family proteins, such as Drosophila melanogaster NCD, budding yeast KAR3, and Arabidopsis thaliana ATK5, walk in the opposite direction, toward microtubule minus ends.[21]

A different type of motor protein known as dyneins, move towards the minus end of the microtubule. Thus they transport cargo from the periphery of the cell towards the centre, for example from the terminal boutons of a neuronal axon to the cell body (soma). This is known as retrograde transport.

Cin8, a member of the Kinesin-5 family, has the novel ability to switch directionality. It has been shown to be minus-end-directed (contrary to the rest of the known Kinesins) when bound to a single microtubule, but plus-end-directed when cross-linking antiparallel microtubules (pushing the minus ends further apart and pulling the plus ends towards each other). This dual directionality has been observed in identical conditions where free Cin8 molecules move towards the minus end, but cross-linking Cin8 move toward the plus ends of each cross-linked microtubule. It is suggested that this unique ability is a result of coupling with other Cin8 motors and helps to fulfill the role of dynein in budding yeast.[22]

Proposed mechanisms of movement

Kinesin accomplishes transport by "walking" along a microtubule. Two mechanisms have been proposed to account for this movement.

  • In the "hand-over-hand" mechanism, the kinesin heads step past one another, alternating the lead position.
  • In the "inchworm" mechanism, one kinesin head always leads, moving forward a step before the trailing head catches up.

Despite some remaining controversy, mounting experimental evidence points towards the hand-over-hand mechanism as being more likely.[23][24]

ATP binding and hydrolysis cause kinesin to travel via a "seesaw mechanism" about a pivot point.[25][26] This seesaw mechanism accounts for observations that the binding of the ATP to the no-nucleotide, microtubule-bound state results in a tilting of the kinesin motor domain relative to the microtubule. Critically, prior to this tilting the neck linker is unable to adopt its motor-head docked, forward-facing conformation. The ATP-induced tilting provides the opportunity for the neck linker to dock in this forward-facing conformation. This model is based on CRYO-EM models of the microtubule-bound kinesin structure which represent the beginning and end states of the process, but cannot resolve the precise details of the transition between the structures.

Theoretical modeling of kinesin

A number of theoretical models of the molecular motor protein Kinesin have been proposed.[27][28][29] Many challenges are encountered in theoretical investigations given the remaining uncertainties about the roles of protein structures, precise way energy from ATP is transformed into mechanical work, and the roles played by thermal fluctuations. This is a rather active area of research. There is a need especially for approaches which better make a link with the molecular architecture of the protein and data obtained from experimental investigations.

Kinesin and mitosis

In recent years, it has been found that microtubule-based molecular motors (including a number of kinesins) have a role in mitosis (cell division). Kinesins are important for proper spindle length and are involved in sliding microtubules apart within the spindle during prometaphase and metaphase, as well as depolymerizing microtubule minus ends at centrosomes during anaphase.[30] Specifically, Kinesin-5 family proteins act within the spindle to slide microtubules apart, while the Kinesin 13 family act to depolymerize microtubules.

Kinesin Superfamily members

Human kinesin superfamily members include the following proteins, which in the standardized nomenclature developed by the community of kinesin researchers, are organized into 14 families named kinesin-1 through kinesin-14:[10]

kinesin-1 light chains:

kinesin-2 associated protein:

  • KAP-1, KAP3 or KIFAP3

See also

References

  1. ^ Vale RD (February 2003). "The molecular motor toolbox for intracellular transport". Cell 112 (4): 467–80. doi:10.1016/S0092-8674(03)00111-9. PMID 12600311. 
  2. ^ Vale RD, Reese TS, Sheetz MP (August 1985). "Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility". Cell 42 (1): 39–50. doi:10.1016/S0092-8674(85)80099-4. PMC 2851632. PMID 3926325. 
  3. ^ Cole DG, Chinn SW, Wedaman KP, Hall K, Vuong T, Scholey JM (November 1993). "Novel heterotrimeric kinesin-related protein purified from sea urchin eggs". Nature 366 (6452): 268–70. Bibcode:1993Natur.366..268C. doi:10.1038/366268a0. PMID 8232586. 
  4. ^ Rosenbaum JL, Witman GB (November 2002). "Intraflagellar transport". Nat. Rev. Mol. Cell Biol. 3 (11): 813–25. doi:10.1038/nrm952. PMID 12415299. 
  5. ^ Yang JT, Laymon RA, Goldstein LS (March 1989). "A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses". Cell 56 (5): 879–89. doi:10.1016/0092-8674(89)90692-2. PMID 2522352. 
  6. ^ Aizawa H, Sekine Y, Takemura R, Zhang Z, Nangaku M, Hirokawa N (December 1992). "Kinesin family in murine central nervous system". J. Cell Biol. 119 (5): 1287–96. doi:10.1083/jcb.119.5.1287. PMC 2289715. PMID 1447303. 
  7. ^ Enos AP, Morris NR (March 1990). "Mutation of a gene that encodes a kinesin-like protein blocks nuclear division in A. nidulans". Cell 60 (6): 1019–27. doi:10.1016/0092-8674(90)90350-N. PMID 2138511. 
  8. ^ Meluh PB, Rose MD (March 1990). "KAR3, a kinesin-related gene required for yeast nuclear fusion". Cell 60 (6): 1029–41. doi:10.1016/0092-8674(90)90351-E. PMID 2138512. 
  9. ^ Hirokawa N, Noda Y, Tanaka Y, Niwa S (October 2009). "Kinesin superfamily motor proteins and intracellular transport". Nat. Rev. Mol. Cell Biol. 10 (10): 682–96. doi:10.1038/nrm2774. PMID 19773780. 
  10. ^ a b Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, Goldstein LS, Goodson HV, Hirokawa N, Howard J, Malmberg RL, McIntosh JR, Miki H, Mitchison TJ, Okada Y, Reddy AS, Saxton WM, Schliwa M, Scholey JM, Vale RD, Walczak CE, Wordeman L (October 2004). "A standardized kinesin nomenclature". J. Cell Biol. 167 (1): 19–22. doi:10.1083/jcb.200408113. PMC 2041940. PMID 15479732. 
  11. ^ Hirokawa N, Pfister KK, Yorifuji H, Wagner MC, Brady ST, Bloom GS (March 1989). "Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration". Cell 56 (5): 867–78. doi:10.1016/0092-8674(89)90691-0. PMID 2522351. 
  12. ^ PDB 1BG2; Kull FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD (April 1996). "Crystal structure of the kinesin motor domain reveals a structural similarity to myosin". Nature 380 (6574): 550–5. Bibcode:1996Natur.380..550J. doi:10.1038/380550a0. PMC 2851642. PMID 8606779. 
  13. ^ Schnitzer MJ, Block SM (1997). "Kinesin hydrolyses one ATP per 8-nm step". Nature 388 (6640): 386–390. Bibcode:1997Natur.388..386S. doi:10.1038/41111. PMID 9237757. 
  14. ^ Vale RD, Milligan RA (April 2000). "The way things move: looking under the hood of molecular motor proteins". Science 288 (5463): 88–95. Bibcode:2000Sci...288...88V. doi:10.1126/science.288.5463.88. PMID 10753125. 
  15. ^ Mather WH, Fox RF (October 2006). "Kinesin's biased stepping mechanism: amplification of neck linker zippering". Biophys. J. 91 (7): 2416–26. Bibcode:2006BpJ....91.2416M. doi:10.1529/biophysj.106.087049. PMC 1562392. PMID 16844749. 
  16. ^ Gross SP, Vershinin M, Shubeita GT (June 2007). "Cargo transport: two motors are sometimes better than one". Current Biology : CB 17 (12): R478–86. doi:10.1016/j.cub.2007.04.025. PMID 17580082. 
  17. ^ Hancock WO (August 2008). "Intracellular transport: kinesins working together". Current Biology : CB 18 (16): R715–7. doi:10.1016/j.cub.2008.07.068. PMID 18727910. 
  18. ^ Kunwar A, Vershinin M, Xu J, Gross SP (August 2008). "Stepping, strain gating, and an unexpected force-velocity curve for multiple-motor-based transport". Current Biology : CB 18 (16): 1173–83. doi:10.1016/j.cub.2008.07.027. PMC 3385514. PMID 18701289. 
  19. ^ Klumpp S, Lipowsky R (November 2005). "Cooperative cargo transport by several molecular motors". Proceedings of the National Academy of Sciences of the United States of America 102 (48): 17284–9. arXiv:q-bio/0512011. Bibcode:2005PNAS..10217284K. doi:10.1073/pnas.0507363102. PMC 1283533. PMID 16287974. 
  20. ^ Rice S, Lin AW, Safer D, Hart CL, Naber N, Carragher BO, Cain SM, Pechatnikova E, Wilson-Kubalek EM, Whittaker M, Pate E, Cooke R, Taylor EW, Milligan RA, Vale RD (December 1999). "A structural change in the kinesin motor protein that drives motility". Nature 402 (6763): 778–84. Bibcode:1999Natur.402..778R. doi:10.1038/45483. PMID 10617199. 
  21. ^ Ambrose JC, Li W, Marcus A, Ma H, Cyr R (April 2005). "A minus-end-directed kinesin with plus-end tracking protein activity is involved in spindle morphogenesis". Mol. Biol. Cell 16 (4): 1584–92. doi:10.1091/mbc.E04-10-0935. PMC 1073643. PMID 15659646. 
  22. ^ Roostalu, J.; Hentrich, C.; Bieling, P.; Telley, I. A.; Schiebel, E.; Surrey, T. (2011). "Directional Switching of the Kinesin Cin8 Through Motor Coupling". Science 332 (6025): 94–99. doi:10.1126/science.1199945. 
  23. ^ Yildiz A, Tomishige M, Vale RD, Selvin PR (2004). "Kinesin Walks Hand-Over-Hand". Science 303 (5658): 676–8. Bibcode:2004Sci...303..676Y. doi:10.1126/science.1093753. PMID 14684828. 
  24. ^ Asbury CL (2005). "Kinesin: world’s tiniest biped". Current Opinion in Cell Biology 17 (1): 89–97. doi:10.1016/j.ceb.2004.12.002. PMID 15661524. 
  25. ^ Sindelar CV, Downing KH (February 2010). "An atomic-level mechanism for activation of the kinesin molecular motors". Proc Natl Acad Sci U S A 107 (9): 4111–6. Bibcode:2010PNAS..107.4111S. doi:10.1073/pnas.0911208107. PMC 2840164. PMID 20160108. 
  26. ^ Lay Summary (18 February 2010). "Life’s smallest motor, cargo carrier of the cells, moves like a seesaw". PhysOrg.com. Retrieved 31 May 2013. 
  27. ^ Atzberger PJ, Peskin CS (January 2006). "A Brownian Dynamics model of kinesin in three dimensions incorporating the force-extension profile of the coiled-coil cargo tether". Bull. Math. Biol. 68 (1): 131–60. doi:10.1007/s11538-005-9003-6. PMID 16794924. 
  28. ^ Peskin CS, Oster G (April 1995). "Coordinated hydrolysis explains the mechanical behavior of kinesin". Biophys. J. 68 (4 Suppl): 202S–210S; discussion 210S–211S. PMC 1281917. PMID 7787069. 
  29. ^ Mogilner A, Fisher AJ, Baskin RJ (July 2001). "Structural changes in the neck linker of kinesin explain the load dependence of the motor's mechanical cycle". J. Theor. Biol. 211 (2): 143–57. doi:10.1006/jtbi.2001.2336. PMID 11419956. 
  30. ^ Goshima G, Vale RD (August 2005). "Cell cycle-dependent dynamics and regulation of mitotic kinesins in Drosophila S2 cells". Mol. Biol. Cell 16 (8): 3896–907. doi:10.1091/mbc.E05-02-0118. PMC 1182325. PMID 15958489. 

Further reading

External links

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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 EPMC: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 EPMC:9428521


External database links

This tab holds annotation information from the InterPro database.

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.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Pfam Clan

This family is a member of clan P-loop_NTPase (CL0023), which has the following description:

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].

The clan contains the following 198 members:

6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_4 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_2 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 CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DUF1253 DUF1611 DUF2075 DUF2478 DUF258 DUF2791 DUF2813 DUF3584 DUF463 DUF815 DUF853 DUF87 DUF927 Dynamin_N Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GTP_EFTU GTP_EFTU_D2 GTP_EFTU_D4 Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD Herpes_Helicase Herpes_ori_bp Herpes_TK IIGP IPPT IPT IstB_IS21 KaiC KAP_NTPase Kinesin Kinesin-relat_1 Kinesin-related KTI12 LpxK MCM MEDS Mg_chelatase Mg_chelatase_2 MipZ Miro MMR_HSR1 MobB MukB MutS_V Myosin_head NACHT NB-ARC NOG1 NTPase_1 ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK Rad17 Rad51 Ras RecA ResIII RHD3 RHSP RNA12 RNA_helicase RuvB_N SbcCD_C SecA_DEAD Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2_N Spore_IV_A SRP54 SRPRB Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulphotransf T2SE T4SS-DNA_transf Terminase_1 Terminase_3 Terminase_6 Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind UPF0079 UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YhjQ Zeta_toxin Zot

Alignments

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(509)
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(2295)
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  Seed
(84)
Full
(9740)
Representative proteomes NCBI
(9371)
Meta
(509)
RP15
(2295)
RP35
(3451)
RP55
(4869)
RP75
(6035)
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  Seed
(84)
Full
(9740)
Representative proteomes NCBI
(9371)
Meta
(509)
RP15
(2295)
RP35
(3451)
RP55
(4869)
RP75
(6035)
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Trees

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Curation and family details

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Seed source: Prosite
Previous IDs: kinesin;
Type: Domain
Author: Bateman A, Finn RD
Number in seed: 84
Number in full: 9740
Average length of the domain: 290.90 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 34.34 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 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: 335
Family (HMM) version: 18
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Species distribution

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Interactions

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

Tubulin Kinesin 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 PDBe 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. There are 149 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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