Tubulin_CTubulin/FtsZ family, C-terminal domain |
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| SMART accession number: | SM00865 |
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| Description: | This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and 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 can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain. |
| Interpro abstract (IPR018316): | This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and 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 can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain. |
| Family alignment: |
There are 36892 Tubulin_C domains in 36813 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Taxonomic distribution of proteins containing Tubulin_C domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Tubulin_C domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Tubulin_C domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
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Cellular role: replication
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Lowe J, Amos LA
- Crystal structure of the bacterial cell-division protein FtsZ.
- Nature. 1998; 391: 203-6
- Display abstract
Bacterial cell division ends with septation, the constriction of the cellwall and cell membranes that leads to the formation of two daughter cells.During septation, FtsZ, a protein of relative molecular mass 40,000 whichis ubiquitous in eubacteria and is also found in archaea and chloroplasts,localizes early at the division site to form a ring-shaped septum. Thisseptum is required for the mechanochemical process of membraneconstriction. FtsZ is a GTPase with weak sequence homology to tubulins.The nature of FtsZ polymers in vivo is unknown, but FtsZ can form tubules,sheets and minirings in vitro. Here we report the crystal structure at 2.8A resolution of recombinant FtsZ from the hyperthermophilic methanogenMethanococcus jannaschii. FtsZ has two domains, one of which is a GTPasedomain with a fold related to one found in the proteins p21ras andelongation factor EF-Tu. The carboxy-terminal domain, whose function isunknown, is a four-stranded beta-sheet tilted by 90 degrees against thebeta-sheet of the GTPase domain. The two domains are arranged around acentral helix. GDP binding is different from that typically found inGTPases and involves four phosphate-binding loops and a sugar-binding loopin the first domain, with guanine being recognized by residues in thecentral connecting helix. The three-dimensional structure of FtsZ issimilar to the structure of alpha- and beta-tubulin.
- Nogales E, Wolf SG, Downing KH
- Structure of the alpha beta tubulin dimer by electron crystallography.
- Nature. 1998; 391: 199-203
- Display abstract
The alphabeta tubulin heterodimer is the structural subunit ofmicrotubules, which are cytoskeletal elements that are essential forintracellular transport and cell division in all eukaryotes. Each tubulinmonomer binds a guanine nucleotide, which is nonexchangeable when it isbound in the alpha subunit, or N site, and exchangeable when bound in thebeta subunit, or E site. The alpha- and beta-tubulins share 40% amino-acidsequence identity, both exist in several isotype forms, and both undergo avariety of posttranslational modifications. Limited sequence homology hasbeen found with the proteins FtsZ and Misato, which are involved in celldivision in bacteria and Drosophila, respectively. Here we present anatomic model of the alphabeta tubulin dimer fitted to a 3.7-A density mapobtained by electron crystallography of zinc-induced tubulin sheets. Thestructures of alpha- and beta-tubulin are basically identical: eachmonomer is formed by a core of two beta-sheets surrounded byalpha-helices. The monomer structure is very compact, but can be dividedinto three functional domains: the amino-terminal domain containing thenucleotide-binding region, an intermediate domain containing theTaxol-binding site, and the carboxy-terminal domain, which probablyconstitutes the binding surface for motor proteins.
- Structure (3D structures containing this domain)
3D Structures of Tubulin_C domains in PDB
PDB code Main view Title 1ffx 
TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX 1fsz 
CRYSTAL STRUCTURE OF THE CELL-DIVISION PROTEIN FTSZ AT 2.8A RESOLUTION 1ia0 
KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM 1jff 
Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol 1ofu 
Crystal structure of SulA:FtsZ from Pseudomonas aeruginosa 1rlu 
Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S 1rq2 
MYCOBACTERIUM TUBERCULOSIS FTSZ IN COMPLEX WITH CITRATE 1rq7 
MYCOBACTERIUM TUBERCULOSIS FTSZ IN COMPLEX WITH GDP 1sa0 
TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX 1sa1 
Tubulin-podophyllotoxin: stathmin-like domain complex 1tub 
TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION 1tvk 
The binding mode of epothilone A on a,b-tubulin by electron crystallography 1w58 
FtsZ GMPCPP soak I213 (M. jannaschii) 1w59 
FtsZ dimer, empty (M. jannaschii) 1w5a 
FtsZ dimer, MgGTP soak (M. jannaschii) 1w5b 
FtsZ dimer, GTP soak (M. jannaschii) 1w5e 
FtsZ W319Y mutant, P1 (M. jannaschii) 1w5f 
FtsZ, T7 mutated, domain swapped (T. maritima) 1z2b 
Tubulin-colchicine-vinblastine: stathmin-like domain complex 1z5v 
Crystal structure of human gamma-tubulin bound to GTPgammaS 1z5w 
Crystal Structure of gamma-tubulin bound to GTP 2btq 
Structure of BtubAB heterodimer from Prosthecobacter dejongeii 2hxf 
KIF1A head-microtubule complex structure in amppnp-form 2hxh 
KIF1A head-microtubule complex structure in adp-form 2p4n 
Human Monomeric Kinesin (1BG2) and Bovine Tubulin (1JFF) Docked into the 9-Angstrom Cryo-EM Map of Nucleotide-Free Kinesin Complexed to the Microtubule 2q1x 
Crystal Structure of cell division protein FtsZ from Mycobacterium tuberculosis in complex with citrate. 2q1y 
Crystal Structure of cell division protein FtsZ from Mycobacterium tuberculosis in complex with GTP-gamma-S 2r6r 
Aquifex aeolicus FtsZ 2r75 
Aquifex aeolicus FtsZ with 8-morpholino-GTP 2rhh 
Synthetic Gene Encoded Bacillus Subtilis FtsZ with Bound Sulfate Ion 2rhj 
Synthetic Gene Encoded Bacillus Subtilis FtsZ with Two Sulfate Ions and Sodium Ion in the Nucleotide Pocket 2rhl 
Synthetic Gene Encoded Bacillus Subtilis FtsZ NCS Dimer with Bound GDP 2rho 
Synthetic Gene Encoded Bacillus Subtilis FtsZ NCS Dimer with Bound GDP and GTP-gamma-S 2vam 
FtsZ B. subtilis 2vap 
FtsZ GDP M. jannaschii 2vaw 
FtsZ Pseudomonas aeruginosa GDP 2vxy 
The structure of FTsZ from Bacillus subtilis at 1.7A resolution 2wbe 
Kinesin-5-Tubulin Complex with AMPPNP 2xrp 
Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules 3cb2 
Crystal structure of human gamma-tubulin bound to GDP 3dco 
Drosophila NOD (3DC4) and Bovine Tubulin (1JFF) Docked into the 11-Angstrom Cryo-EM Map of Nucleotide-Free NOD Complexed to the Microtubule 3du7 
Tubulin-colchicine-phomopsin A: Stathmin-like domain complex 3e22 
Tubulin-colchicine-soblidotin: Stathmin-like domain complex 3edl 
Kinesin13-Microtubule Ring complex 3hkb 
Tubulin: RB3 Stathmin-like domain complex 3hkc 
Tubulin-ABT751: RB3 stathmin-like domain complex 3hkd 
Tubulin-TN16 : RB3 stathmin-like domain complex 3hke 
Tubulin-T138067: RB3 stathmin-like domain complex 3iz0 
Human Ndc80 Bonsai Decorated Microtubule 3j1t 
High affinity dynein microtubule binding domain - tubulin complex 3j1u 
Low affinity dynein microtubule binding domain - tubulin complex 3j2u 
Kinesin-13 KLP10A HD in complex with CS-tubulin and a microtubule 3j6e 
3J6E 3j6f 
3J6F 3j6g 
3J6G 3j6h 
3J6H 3j6p 
3J6P 3j7i 
3J7I 3j8x 
3J8X 3j8y 
3J8Y 3jak 
3JAK 3jal 
3JAL 3jao 
3JAO 3jar 
3JAR 3jas 
3JAS 3jat 
3JAT 3jaw 
3JAW 3n2g 
TUBULIN-NSC 613863: RB3 Stathmin-like domain complex 3n2k 
TUBULIN-NSC 613862: RB3 Stathmin-like domain complex 3ryc 
Tubulin: RB3 stathmin-like domain complex 3ryf 
GTP-Tubulin: RB3 Stathmin-like domain complex 3ryh 
GMPCPP-Tubulin: RB3 Stathmin-like domain complex 3ryi 
GDP-Tubulin: rb3 stathmin-like domain complex 3ut5 
Tubulin-Colchicine-Ustiloxin: Stathmin-like domain complex 3vo8 
Staphylococcus aureus FtsZ GDP-form 3vo9 
Staphylococcus aureus FtsZ apo-form (SeMet) 3voa 
Staphylococcus aureus FtsZ 12-316 GDP-form 3vob 
Staphylococcus aureus FtsZ with PC190723 3vpa 
Staphylococcus aureus FtsZ apo-form 3wgj 
STAPHYLOCOCCUS AUREUS FTSZ T7 chimera mutant, T7Bs 3wgk 
STAPHYLOCOCCUS AUREUS FTSZ T7 mutant substituted for GAG, DeltaT7GAG-GDP 3wgl 
STAPHYLOCOCCUS AUREUS FTSZ T7 mutant substituted for GAN bound with GDP, DeltaT7GAN-GDP 3wgm 
STAPHYLOCOCCUS AUREUS FTSZ T7 mutant substituted for GAN bound with GTP, DeltaT7GAN-GTP 3wgn 
STAPHYLOCOCCUS AUREUS FTSZ bound with GTP-gamma-S 4abo 
Mal3 CH domain homology model and mammalian tubulin (2XRP) docked into the 8.6-Angstrom cryo-EM map of Mal3-GTPgammaS-microtubules 4aqv 
Model of human kinesin-5 motor domain (3HQD) and mammalian tubulin heterodimer (1JFF) docked into the 9.7-angstrom cryo-EM map of microtubule-bound kinesin-5 motor domain in the AMPPPNP state. 4aqw 
Model of human kinesin-5 motor domain (1II6, 3HQD) and mammalian tubulin heterodimer (1JFF) docked into the 9.5-angstrom cryo-EM map of microtubule-bound kinesin-5 motor domain in the rigor state. 4atu 
Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM map of doublecortin-stabilised microtubules reconstructed in absence of kinesin 4atx 
Rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8A cryo-EM map of doublecortin- microtubules decorated with kinesin 4ck5 
Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP state, based on cryo-electron microscopy experiment. 4ck6 
Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state, based on cryo-electron microscopy experiment. 4ck7 
Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in presence of adp.alfx (NECK-LINKER IN ITS DISCONNECTED CONFORMATION, based on cryo-electron microscopy experiment 4drx 
GTP-Tubulin in complex with a DARPIN 4dxd 
Staphylococcal Aureus FtsZ in complex with 723 4e6e 
Crystal structure of a putative cell division protein FtsZ (Tfu_1113) from Thermobifida fusca YX-ER1 at 2.22 A resolution (PSI Community Target, van Wezel G.P.) 4eb6 
Tubulin-Vinblastine: Stathmin-like complex 4f61 
Tubulin:Stathmin-like domain complex 4f6r 
Tubulin:Stathmin-like domain complex 4ffb 
A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a Microtubule Polymerase 4hna 
Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN 4i4t 
Crystal structure of tubulin-RB3-TTL-Zampanolide complex 4i50 
Crystal structure of tubulin-stathmin-TTL-Epothilone A complex 4i55 
Crystal structure of tubulin-stathmin-TTL complex 4ihj 
Crystal structure of tubulin-stathmin-TTL-ADP complex 4iij 
Crystal structure of tubulin-stathmin-TTL-apo complex 4kwe 
GDP-bound, double-stranded, curved FtsZ protofilament structure 4lnu 
4LNU 4m8i 
1.43 Angstrom resolution crystal structure of cell division protein FtsZ (ftsZ) from Staphylococcus epidermidis RP62A in complex with GDP 4o2a 
Tubulin-BAL27862 complex 4o2b 
Tubulin-Colchicine complex 4o4h 
Tubulin-Laulimalide complex 4o4i 
Tubulin-Laulimalide-Epothilone A complex 4o4j 
Tubulin-Peloruside A complex 4o4l 
Tubulin-Peloruside A-Epothilone A complex 4tuy 
4TUY 4tv8 
4TV8 4tv9 
4TV9 4u39 
4U39 4u3j 
4U3J 4uxo 
4UXO 4uxp 
4UXP 4uxr 
4UXR 4uxs 
4UXS 4uxt 
4UXT 4uxy 
4UXY 4uy0 
4UY0 4wbn 
4WBN 4x1i 
4X1I 4x1k 
4X1K 4x1y 
4X1Y 4x20 
4X20 4yj2 
4YJ2 4yj3 
4YJ3 4zhq 
4ZHQ 4zi7 
4ZI7 4zol 
4ZOL 5bmv 
5BMV 5c8y 
5C8Y 5ca0 
5CA0 5ca1 
5CA1 5cb4 
5CB4 5eib 
5EIB 5eyp 
5EYP 5flz 
5FLZ 5fm1 
5FM1 5fnv 
5FNV 5hnw 
5HNW 5hnx 
5HNX 5hny 
5HNY 5hnz 
5HNZ 5ij0 
5IJ0 5ij9 
5IJ9 5itz 
5ITZ 5iyz 
5IYZ 5j2t 
5J2T 5j2u 
5J2U 5jco 
5JCO 5jh7 
5JH7 5jqg 
5JQG 5jvd 
5JVD 5kmg 
5KMG 5la6 
5LA6 5lov 
5LOV 5lp6 
5LP6 5m5i 
5M5I 5m5l 
5M5L 5m5m 
5M5M 5m5n 
5M5N 5m5o 
5M5O - Links (links to other resources describing this domain)
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PFAM Tubulin_C INTERPRO IPR018316