Summary: Tubulin/FtsZ family, GTPase domain
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.
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
|Similarity to PfamA using HHSearch:||Tubulin_2 Tubulin_3|
External database links
|PROSITE:||PDOC00199 PDOC00200 PDOC00873|
This tab holds annotation information from the InterPro database.
InterPro entry IPR003008
This domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. 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, this entry is the GTPase domain. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||protein complex (GO:0043234)|
|Biological process||protein polymerization (GO:0051258)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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This superfamily is characterised by being of alpha-beta two-layer sandwich structures. 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 .
The clan contains the following 6 members:FtsZ_C Misat_Tub_SegII Tubulin Tubulin_2 Tubulin_3 Tubulin_C
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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Curation and family details
|Author:||Bateman A, Sonnhammer ELL, Griffiths-Jones SR|
|Number in seed:||94|
|Number in full:||20546|
|Average length of the domain:||152.80 aa|
|Average identity of full alignment:||36 %|
|Average coverage of the sequence by the domain:||51.77 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||20|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 170 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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