The domain within your query sequence starts at position 586 and ends at position 818; the E-value for the TOG domain shown below is 1.29e-69.
ELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMERTEMPCQALVKMLA KKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQIVLDGLVDKIGDVKCGNNAKEAMTA IAEACMLPWTAEQVMSMAFSQKNPKNQSETLNWLSNAIKEFGFSELNVKAFISNVKTALA ATNPAVRTSAITLLGVMYLYVGPSLRMIFEDEKPALLSQIDAEFQKMQGQSPP
TOG |
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SMART accession number: | SM01349 |
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Description: | XMAP215/Dis1 proteins, such as Alp14 and XMAP215, increase microtubules dynamic polymerization rates by recruiting soluble αβ-tubulin via their conserved TOG domains to polymerizing microtubule plus ends. |
Interpro abstract (IPR034085): | This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis [ (PUBMED:10361086) ]. These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains, including the armadillo repeat (found in beta-catenins and importins), the HEAT repeat (found in protein phosphatase 2a and initiation factor eIF4G), the PHAT domain (found in Smaug RNA-binding protein), the leucine-rich repeat variant, the Pumilo repeat, and in the H regulatory subunit of V-type ATPases. The sequence similarity among these different repeats or domains is low, however they exhibit considerable structural similarity. Furthermore, the number of repeats present in the superhelical structure can vary between orthologues, indicating that rapid loss/gain of repeats has occurred frequently in evolution. A common phylogenetic origin has been proposed for the armadillo and HEAT repeats [ (PUBMED:11551174) ]. This entry represents a structural domain with an armadillo (ARM)-like fold, consisting of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis [ (PUBMED:10361086) ]. These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. Domains and repeats with an ARM-like fold have been found in a number of proteins, including:
The sequence similarity among these different repeats or domains is low, however they exhibit considerable structural similarity. Furthermore, the number of repeats present in the superhelical structure can vary between orthologues, indicating that rapid loss/gain of repeats has occurred frequently in evolution. A common phylogenetic origin has been proposed for the armadillo and HEAT repeats [ (PUBMED:11551174) ]. XMAP215/Dis1 proteins, such as Alp14 and XMAP215, increase microtubules dynamic polymerization rates by recruiting soluble alpha/beta-tubulin via their conserved TOG domains to polymerizing microtubule plus ends [ (PUBMED:21782439) (PUBMED:24630105) ]. A TOG domain contains HEAT repeats. |
Family alignment: |
There are 20108 TOG domains in 5624 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)