Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR022768 is a Fascin-like domain.
<p>This entry represents the fascin-like domain, which is found repeated four times in members of the fascin family. This domain adopts a β-trefoil fold [[cite:PUB00065219]].</p> <p>The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture [[cite:PUB00012306]]. Dictyostelium hisactophilin, another actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerisation and binding to microfilaments only at pH values below seven [[cite:PUB00012306]]. Members of this group are histidine rich, typically contain the repeated motif of HHXH [[cite:PUB00012367]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
GO term | Namespace | Name | Definition | Relationships |
---|---|---|---|---|
Molecular function | Protein binding, bridging | The binding activity of a molecule that brings together two or more protein molecules, or a protein and another macromolecule or complex, through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. | ||
Molecular function | Actin filament binding | Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | Glucan 1,3-beta-glucosidase [Medicago truncatula] gi|357463267|ref|XP_003601915.1| | 25 | ||
– | Glucan 1,3-beta-glucosidase; TAIR: AT4G39170.1 Sec14p-like phosphatidylinositol transfer family protein; Swiss-Prot: sp|B0XN12|EXGA_ASPFC Probable glucan 1,3-beta-glucosidase A; TrEMBL-Plants: tr|V7D1X4|V7D1X4_PHAVU Uncharacterized protein; Found in the gene: LotjaGi6g1v0090500 | 22 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
TRANSMEMBRANE | Phobius | 1 | 50.00 |