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2701  structures 8702  species 0  interactions 31772  sequences 367  architectures

Family: Tubulin (PF00091)

Summary: Tubulin/FtsZ family, GTPase domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

Tubulin Edit Wikipedia article

Tubulin
PDB 1ia0 EBI.jpg
kif1a head-microtubule complex structure in atp-form
Identifiers
SymbolTubulin
PfamPF00091
Pfam clanCL0442
InterProIPR003008
PROSITEPDOC00201
SCOP21tub / SCOPe / SUPFAM

Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton.[1] Microtubules function in many essential cellular processes, including mitosis. Tubulin-binding drugs kill cancerous cells by inhibiting microtubule dynamics, which are required for DNA segregation and therefore cell division.

In eukaryotes there are six members of the tubulin superfamily, although not all are present in all species (see below).[2][3] Both α and β tubulins have a mass of around 50 kDa and are thus in a similar range compared to actin (with a mass of ~42 kDa). In contrast, tubulin polymers (microtubules) tend to be much bigger than actin filaments due to their cylindrical nature.

Tubulin was long thought to be specific to eukaryotes. More recently, however, several prokaryotic proteins have been shown to be related to tubulin.[4][5][6][7]

Characterization

Tubulin is characterized by the evolutionarily conserved Tubulin/FtsZ family, GTPase protein domain.

This GTPase protein domain is found in all eukaryotic tubulin chains,[8] as well as the bacterial protein TubZ,[7] the archaeal protein CetZ,[9] and the FtsZ protein family widespread in Bacteria and Archaea.[4][10]

Function

Microtubules

Tubulin and Microtubule Metrics Infographic
Tubulin and microtubule metrics [11]

α- and β-tubulin polymerize into dynamic microtubules. In eukaryotes, microtubules are one of the major components of the cytoskeleton, and function in many processes, including structural support, intracellular transport, and DNA segregation.

Comparison of the architectures of a 5-protofilament bacterial microtubule (left; BtubA in dark blue; BtubB in light-blue) and a 13-protofilament eukaryotic microtubule (right; α-tubulin in white; β-tubulin in black). Seams and start-helices are indicated in green and red, respectively.[12]

Microtubules are assembled from dimers of α- and β-tubulin. These subunits are slightly acidic with an isoelectric point between 5.2 and 5.8.[13] Each has a molecular weight of approximately 50 kDa.[14]

To form microtubules, the dimers of α- and β-tubulin bind to GTP and assemble onto the (+) ends of microtubules while in the GTP-bound state.[15] The β-tubulin subunit is exposed on the plus end of the microtubule while the α-tubulin subunit is exposed on the minus end. After the dimer is incorporated into the microtubule, the molecule of GTP bound to the β-tubulin subunit eventually hydrolyzes into GDP through inter-dimer contacts along the microtubule protofilament.[16] The GTP molecule bound to the α-tubulin subunit is not hydrolyzed during the whole process. Whether the β-tubulin member of the tubulin dimer is bound to GTP or GDP influences the stability of the dimer in the microtubule. Dimers bound to GTP tend to assemble into microtubules, while dimers bound to GDP tend to fall apart; thus, this GTP cycle is essential for the dynamic instability of the microtubule.

Bacterial microtubules

Homologs of α- and β-tubulin have been identified in the Prosthecobacter genus of bacteria.[5] They are designated BtubA and BtubB to identify them as bacterial tubulins. Both exhibit homology to both α- and β-tubulin.[17] While structurally highly similar to eukaryotic tubulins, they have several unique features, including chaperone-free folding and weak dimerization.[18] Cryogenic electron microscopy showed that BtubA/B forms microtubules in vivo, and suggested that these microtubules comprise only five protofilaments, in contrast to eukaryotic microtubules, which usually contain 13.[12] Subsequent in vitro studies have shown that BtubA/B forms four-stranded 'mini-microtubules'.[19]

Prokaryotic division

FtsZ is found in nearly all Bacteria and Archaea, where it functions in cell division, localizing to a ring in the middle of the dividing cell and recruiting other components of the divisome, the group of proteins that together constrict the cell envelope to pinch off the cell, yielding two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro, and forms dynamic filaments in vivo.

TubZ functions in segregating low copy-number plasmids during bacterial cell division. The protein forms a structure unusual for a tubulin homolog; two helical filaments wrap around one another.[20] This may reflect an optimal structure for this role since the unrelated plasmid-partitioning protein ParM exhibits a similar structure.[21]

Cell shape

CetZ functions in cell shape changes in pleomorphic Haloarchaea. In Haloferax volcanii, CetZ forms dynamic cytoskeletal structures required for differentiation from a plate-shaped cell form into a rod-shaped form that exhibits swimming motility.[9]

Types

Eukaryotic

The tubulin superfamily contains six families (alpha-(α), beta-(β), gamma-(γ), delta-(δ), epsilon-(ε), and zeta-(ζ) tubulins).[22]

α-Tubulin

Human α-tubulin subtypes include:[citation needed]

β-Tubulin

β-tubulin in Tetrahymena sp.

All drugs that are known to bind to human tubulin bind to β-tubulin.[23] These include paclitaxel, colchicine, and the vinca alkaloids, each of which have a distinct binding site on β-tubulin.[23]

In addition, several anti-worm drugs preferentially target the colchicine site of β-Tubulin in worm rather than in higher eukaryotes. While mebendazole still retains some binding affinity to human and Drosophila β-tubulin,[24] albendazole almost exclusively binds to the β-tubulin of worms and other lower eukaryotes.[25][26]

Class III β-tubulin is a microtubule element expressed exclusively in neurons,[27] and is a popular identifier specific for neurons in nervous tissue. It binds colchicine much more slowly than other isotypes of β-tubulin.[28]

β1-tubulin, sometimes called class VI β-tubulin,[29] is the most divergent at the amino acid sequence level.[30] It is expressed exclusively in megakaryocytes and platelets in humans and appears to play an important role in the formation of platelets.[30] When class VI β-tubulin were expressed in mammalian cells, they cause disruption of microtubule network, microtubule fragment formation, and can ultimately cause marginal-band like structures present in megakaryocytes and platelets.[31]

Katanin is a protein complex that severs microtubules at β-tubulin subunits, and is necessary for rapid microtubule transport in neurons and in higher plants.[32]

Human β-tubulins subtypes include:[citation needed]

γ-Tubulin

Γ-tubulin ring complex (γ-TuRC)

γ-Tubulin, another member of the tubulin family, is important in the nucleation and polar orientation of microtubules. It is found primarily in centrosomes and spindle pole bodies, since these are the areas of most abundant microtubule nucleation. In these organelles, several γ-tubulin and other protein molecules are found in complexes known as γ-tubulin ring complexes (γ-TuRCs), which chemically mimic the (+) end of a microtubule and thus allow microtubules to bind. γ-tubulin also has been isolated as a dimer and as a part of a γ-tubulin small complex (γTuSC), intermediate in size between the dimer and the γTuRC. γ-tubulin is the best understood mechanism of microtubule nucleation, but certain studies have indicated that certain cells may be able to adapt to its absence, as indicated by mutation and RNAi studies that have inhibited its correct expression. Besides forming a γ-TuRC to nucleate and organize microtubules, γ-tubulin can polymerize into filaments that assemble into bundles and meshworks.[33]

Human γ-tubulin subtypes include:

Members of the γ-tubulin ring complex:

δ and ε-Tubulin

Delta (δ) and epsilon (ε) tubulin have been found to localize at centrioles and may play a role in centriole structure and function, though neither is as well-studied as the α- and β- forms.

Human δ- and ε-tubulin genes include:[citation needed]

ζ-Tubulin

Zeta-tubulin (IPR004058) is present in many eukaryotes, but missing from others, including placental mammals. It has been shown to be associated with the basal foot structure of centrioles in multiciliated epithelial cells.[3]

Prokaryotic

BtubA/B

BtubA (Q8GCC5) and BtubB (Q8GCC1) are found in some bacterial species in the Verrucomicrobial genus Prosthecobacter.[5] Their evolutionary relationship to eukaryotic tubulins is unclear, although they may have descended from a eukaryotic lineage by lateral gene transfer.[18][17] Compared to other bacterial homologs, they are much more similar to eukaryotic tubulins. In an assembled structure, BtubB acts like α-tubulin and BtubA acts like β-tubulin.[34]

FtsZ

Many bacterial and euryarchaeotal cells use FtsZ to divide via binary fission. All chloroplasts and some mitochrondria, both organelles derived from endosymbiosis of bacteria, also use FtsZ.[35] It was the first prokaryotic cytoskeletal protein identified.

TubZ

TubZ (Q8KNP3; pBt156) was identified in Bacillus thuringiensis as essential for plasmid maintenance.[7] It binds to a DNA-binding protein called TubR (Q8KNP2; pBt157) to pull the plasmid around.[36]

CetZ

CetZ (D4GVD7) is found in the euryarchaeal clades of Methanomicrobia and Halobacteria, where it functions in cell shape differentiation.[9]

Phage tubulins

Phages of the genus Phikzlikevirus, as well as a Serratia phage PCH45, use a shell protein (Q8SDA8) to build a nucleus-like structure called the phage nucleus. This structure encloses DNA as well as replication and transcription machinery. It protects phage DNA from host defenses like restriction enzymes and type I CRISPR-Cas systems. A spindle-forming tubulin, variously named PhuZ (B3FK34) and gp187, centers the nucleus in the cell.[37][38]

Odinarchaeota tubulin

Asgard archaea tubulin from hydrothermal-living Odinarchaeota (OdinTubulin) was identified as a genuine tubulin. OdinTubulin forms protomers and protofilaments most similar to eukaryotic microtubules, yet assembles into ring systems more similar to FtsZ, indicating that OdinTubulin may represent an evolution intermediate between FtsZ and microtubule-forming tubulins. [39]

Pharmacology

Tubulins are targets for anticancer drugs like the vinca alkaloid drugs[40][41][42] vinblastine and vincristine,[43][44] and paclitaxel.[45] The anti-worm drugs mebendazole and albendazole as well as the anti-gout agent colchicine bind to tubulin and inhibit microtubule formation. While the former ultimately lead to cell death in worms, the latter arrests neutrophil motility and decreases inflammation in humans. The anti-fungal drug griseofulvin targets microtubule formation and has applications in cancer treatment.

Post-translational modifications

When incorporated into microtubules, tubulin accumulates a number of post-translational modifications, many of which are unique to these proteins. These modifications include detyrosination,[46] acetylation, polyglutamylation, polyglycylation, phosphorylation, ubiquitination, sumoylation, and palmitoylation. Tubulin is also prone to oxidative modification and aggregation during, for example, acute cellular injury.[47]

Nowadays there are many scientific investigations of the acetylation done in some microtubules, specially the one by α-tubulin N-acetyltransferase (ATAT1) which is being demonstrated to play an important role in many biological and molecular functions and, therefore, it is also associated with many human diseases, specially neurological diseases.

See also

References

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  2. ^ Findeisen P, Mühlhausen S, Dempewolf S, Hertzog J, Zietlow A, Carlomagno T, Kollmar M "Six subgroups and extensive recent duplications characterize the evolution of the eukaryotic tubulin protein family" Genome Biol Evol (2014) 6:2274-2288.
  3. ^ a b Turk E, Wills AA, Kwon T, Sedzinski J, Wallingford JB, Stearns T "Zeta-Tubulin Is a Member of a Conserved Tubulin Module and Is a Component of the Centriolar Basal Foot in Multiciliated Cells" Current Biology (2015) 25:2177-2183.
  4. ^ a b Nogales E, Downing KH, Amos LA, Löwe J (June 1998). "Tubulin and FtsZ form a distinct family of GTPases". Nature Structural Biology. 5 (6): 451–8. doi:10.1038/nsb0698-451. PMID 9628483. S2CID 5945125.
  5. ^ a b c Jenkins C, Samudrala R, Anderson I, Hedlund BP, Petroni G, Michailova N, et al. (December 2002). "Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 17049–54. Bibcode:2002PNAS...9917049J. doi:10.1073/pnas.012516899. PMC 139267. PMID 12486237.
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  7. ^ a b c Larsen RA, Cusumano C, Fujioka A, Lim-Fong G, Patterson P, Pogliano J (June 2007). "Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis". Genes & Development. 21 (11): 1340–52. doi:10.1101/gad.1546107. PMC 1877747. PMID 17510284.
  8. ^ Nogales E, Wolf SG, Downing KH (January 1998). "Structure of the alpha beta tubulin dimer by electron crystallography". Nature. 391 (6663): 199–203. Bibcode:1998Natur.391..199N. doi:10.1038/34465. PMID 9428769. S2CID 4412367.
  9. ^ a b c Duggin IG, Aylett CH, Walsh JC, Michie KA, Wang Q, Turnbull L, et al. (March 2015). "CetZ tubulin-like proteins control archaeal cell shape". Nature. 519 (7543): 362–5. Bibcode:2015Natur.519..362D. doi:10.1038/nature13983. PMC 4369195. PMID 25533961.
  10. ^ Löwe J, Amos LA (January 1998). "Crystal structure of the bacterial cell-division protein FtsZ". Nature. 391 (6663): 203–6. Bibcode:1998Natur.391..203L. doi:10.1038/34472. PMID 9428770. S2CID 4330857.
  11. ^ "Digital Downloads". PurSolutions. Retrieved 2020-02-19.
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  13. ^ Williams RC, Shah C, Sackett D (November 1999). "Separation of tubulin isoforms by isoelectric focusing in immobilized pH gradient gels". Analytical Biochemistry. 275 (2): 265–7. doi:10.1006/abio.1999.4326. PMID 10552916.
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  23. ^ a b Zhou J, Giannakakou P (January 2005). "Targeting microtubules for cancer chemotherapy". Current Medicinal Chemistry. Anti-Cancer Agents. 5 (1): 65–71. doi:10.2174/1568011053352569. PMID 15720262.
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  28. ^ Ludueña RF (May 1993). "Are tubulin isotypes functionally significant". Molecular Biology of the Cell. 4 (5): 445–57. doi:10.1091/mbc.4.5.445. PMC 300949. PMID 8334301.
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  30. ^ a b Lecine P, et al. (August 2000). "Hematopoietic-specific beta 1 tubulin participates in a pathway of platelet biogenesis dependent on the transcription factor NF-E2". Blood. 96 (4): 1366–73. doi:10.1182/blood.V96.4.1366. PMID 10942379.
  31. ^ Yang H, Ganguly A, Yin S, Cabral F (March 2011). "Megakaryocyte lineage-specific class VI β-tubulin suppresses microtubule dynamics, fragments microtubules, and blocks cell division". Cytoskeleton. 68 (3): 175–87. doi:10.1002/cm.20503. PMC 3082363. PMID 21309084.
  32. ^ McNally FJ, Vale RD (November 1993). "Identification of katanin, an ATPase that severs and disassembles stable microtubules". Cell. 75 (3): 419–29. doi:10.1016/0092-8674(93)90377-3. PMID 8221885. S2CID 10264319.
  33. ^ Chumová J, Trögelová L, Kourová H, Volc J, Sulimenko V, Halada P, Kučera O, Benada O, Kuchařová A, Klebanovych A, Dráber P, Daniel G, Binarová P (2018). "γ-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1865 (5): 734–748. doi:10.1016/j.bbamcr.2018.02.009. PMID 29499229. S2CID 4053150.
  34. ^ Sontag CA, Sage H, Erickson HP (September 2009). "BtubA-BtubB heterodimer is an essential intermediate in protofilament assembly". PLOS ONE. 4 (9): e7253. Bibcode:2009PLoSO...4.7253S. doi:10.1371/journal.pone.0007253. PMC 2746283. PMID 19787042.
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External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Tubulin domain". More...

Tubulin domain Edit Wikipedia article

Tubulin
PDB 1ia0 EBI.jpg
kif1a head-microtubule complex structure in atp-form
Identifiers
SymbolTubulin
PfamPF00091
Pfam clanCL0442
InterProIPR003008
PROSITEPDOC00201
SCOP21tub / SCOPe / SUPFAM
Tubulin
PDB 1ia0 EBI.jpg
kif1a head-microtubule complex structure in atp-form
Identifiers
SymbolTubulin
PfamPF00091
Pfam clanCL0442
InterProIPR003008
PROSITEPDOC00201
SCOP21tub / SCOPe / SUPFAM

Tubulin/FtsZ family, GTPase domain is an evolutionary conserved protein domain.

This domain is found in all tubulin chains,[1] as well as the bacterial FtsZ family of proteins.[2] These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases,[3] this entry is the GTPase domain. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea.

References

  1. ^ Nogales E, Wolf SG, Downing KH (January 1998). "Structure of the alpha beta tubulin dimer by electron crystallography". Nature. 391 (6663): 199–203. doi:10.1038/34465. PMID 9428769. S2CID 4412367.
  2. ^ Löwe J, Amos LA (January 1998). "Crystal structure of the bacterial cell-division protein FtsZ". Nature. 391 (6663): 203–6. doi:10.1038/34472. PMID 9428770. S2CID 4330857.
  3. ^ Nogales E, Downing KH, Amos LA, Löwe J (June 1998). "Tubulin and FtsZ form a distinct family of GTPases". Nat. Struct. Biol. 5 (6): 451–8. doi:10.1038/nsb0698-451. PMID 9628483. S2CID 5945125.
This article incorporates text from the public domain Pfam and InterPro: IPR003008

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Tubulin/FtsZ family, GTPase domain Provide feedback

This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.

Literature references

  1. Nogales E, Wolf SG, Downing KH; , Nature 1998;391:199-203.: Structure of the alphabeta tubulin dimer by electron crystallography. PUBMED:9428769 EPMC:9428769

  2. Nogales E, Downing KH, Amos LA, Lowe J; , Nat Struct Biol 1998;5:451-458.: Tubulin and FtsZ form a distinct family of GTPases. PUBMED:9628483 EPMC:9628483

  3. Lowe J, Amos LA; , Nature 1998;391:203-206.: Crystal structure of the bacterial cell-division protein FtsZ [see comments] PUBMED:9428770 EPMC:9428770

  4. Miklos GL, Yamamoto M, Burns RG, Maleszka R; , Proc Natl Acad Sci U S A. 1997;94:5189-5194.: An essential cell division gene of Drosophila, absent from Saccharomyces, encodes an unusual protein with tubulin-like and myosin-like peptide motifs. PUBMED:9144213 EPMC:9144213


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003008

This entry represents a GTPase domain found in all tubulin chains, such as tubulin alpha, beta and gamma chains, plant ARC3 and prokaryotic FtsZ and CetZ proteins [ PUBMED:9628483 , PUBMED:25339962 ]. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ (homologue of eukaryotic tubulin) is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells [ PUBMED:9144213 , PUBMED:9428770 ]. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. CetZ co-exists with FtsZ in many archaea. Cetz does not affect cell division, instead, it is involved in cell shape control [ PUBMED:25533961 ]. Arabidopsis chloroplast protein ARC3 (At1g75010) is a Z-ring accessory protein involved in the initiation of plastid division and division site placement [ PUBMED:15356321 , PUBMED:18764889 ].

Gene Ontology

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

Domain organisation

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

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Pfam Clan

This family is a member of clan Tubulin (CL0566), which has the following description:

The characteristic families of this clan are the tubulin GTPase domain and the alpha and beta tubulin subunits. A segmental duplication early on in the primate lineage has led to the creation of up to three tubulin-like domains in the higher primates. The most N-terminal one is the Misato domain, which probably represents the original domain [3].

The clan contains the following 4 members:

Misat_Tub_SegII Tubulin Tubulin_2 Tubulin_3

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(87)
Full
(31772)
Representative proteomes UniProt
(120720)
RP15
(6070)
RP35
(14912)
RP55
(27484)
RP75
(40045)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(87)
Full
(31772)
Representative proteomes UniProt
(120720)
RP15
(6070)
RP35
(14912)
RP55
(27484)
RP75
(40045)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(87)
Full
(31772)
Representative proteomes UniProt
(120720)
RP15
(6070)
RP35
(14912)
RP55
(27484)
RP75
(40045)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

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

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's seed alignment. 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 alignment.

Note: You can also download the data file for the tree.

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: tubulin;
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Sonnhammer ELL , Griffiths-Jones SR
Number in seed: 87
Number in full: 31772
Average length of the domain: 177.90 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 42.93 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 33.0 33.0
Trusted cut-off 33.0 33.0
Noise cut-off 32.9 32.9
Model length: 197
Family (HMM) version: 28
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 Tubulin domain has been found. There are 2701 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A096SSY4 View 3D Structure Click here
A0A0G2K6I6 View 3D Structure Click here
A0A0H2UHM7 View 3D Structure Click here
A0A0R0FGR2 View 3D Structure Click here
A0A0R0IHF9 View 3D Structure Click here
A0A0R0JYY8 View 3D Structure Click here
A0A0R4IPH2 View 3D Structure Click here
A0A0R4IXC8 View 3D Structure Click here
A0A143ZWL7 View 3D Structure Click here
A0A1D6F117 View 3D Structure Click here
A0A1D6FAY2 View 3D Structure Click here
A0A1D6FKF1 View 3D Structure Click here
A0A1D6FLE9 View 3D Structure Click here
A0A1D6FLZ8 View 3D Structure Click here
A0A1D6FPC6 View 3D Structure Click here
A0A1D6FQ69 View 3D Structure Click here
A0A1D6FWR4 View 3D Structure Click here
A0A1D6GCF0 View 3D Structure Click here
A0A1D6GG72 View 3D Structure Click here
A0A1D6GG78 View 3D Structure Click here
A0A1D6IX35 View 3D Structure Click here
A0A1D6JIK1 View 3D Structure Click here
A0A1D6JN20 View 3D Structure Click here
A0A1D6K088 View 3D Structure Click here
A0A1D6L4K1 View 3D Structure Click here
A0A1D6L9Y2 View 3D Structure Click here
A0A1D6LI31 View 3D Structure Click here
A0A1D6LNQ1 View 3D Structure Click here
A0A1D6LPW4 View 3D Structure Click here
A0A1D6MR52 View 3D Structure Click here
A0A1D6NQX5 View 3D Structure Click here
A0A1D6NZV3 View 3D Structure Click here
A0A1D6P5U4 View 3D Structure Click here
A0A1D6PYG5 View 3D Structure Click here
A0A1D6QKL8 View 3D Structure Click here
A0A1D6QRH0 View 3D Structure Click here
A0A1D8PC97 View 3D Structure Click here
A0A1D8PMD4 View 3D Structure Click here
A0A1D8PTV4 View 3D Structure Click here
A0A2R8RVU0 View 3D Structure Click here