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 [PMID: 7049841]. Several stress-induced proteins of plants have been found to be related to thaumatins:A maize alpha-amylase/trypsin inhibitor, two tobacco pathogenesis-related proteins: PR-R major and minor forms,which are induced after infection with viruses, Salt-induced protein NP24 from tomato, Osmotin, a salt-induced protein from tobacco [PMID: 16666857], Osmotin-like proteins OSML13, OSML15 and OSML81 from potato [PMID: 7630973], P21, a leaf protein from soybean, PWIR2, a leaf protein from wheat [PMID: 1650615], Zeamatin, a maize antifunal protein [PMID: 7846159]. 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 [PMID: 1463856]. The proteins are involved in systematically acquired resistance and stress response in plants, although their precise role is unknown [PMID: 1463856].

The below sequences were used to create Thaumatin sequence signatures:

The below sequences were retrieved using Thaumatin sequence signatures: