|SMART accession number:||SM00205|
|Description:||The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism.|
|Interpro abstract (IPR001938):|
Thaumatin [(PUBMED:7049841)] is an intensely sweet-tasting protein, 100 000 times sweeter than sucrose on a molar basis [(PUBMED:7049841)] found in berries from Thaumatococcus daniellii, a tropical flowering plant known as Katemfe, it is induced by attack by viroids, which are single-stranded unencapsulated RNA molecules that do not code for protein.
Thaumatin consists of about 200 residues and contains 8 disulphide bonds. Like other PR proteins, thaumatin is predicted to have a mainly beta structure, with a high content of beta-turns and little helix [(PUBMED:7049841)]. Several stress-induced proteins of plants have been found to be related to thaumatins:
This protein is also referred to as pathogenesis-related group 5 (PR5), as many thaumatin-like proteins accumulate in plants in response to infection by a pathogen and possess antifungal activity [(PUBMED:1463856)]. The proteins are involved in systematically acquired resistance and stress response in plants, although their precise role is unknown [(PUBMED:1463856)].
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- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
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