| Description | The host selective cysteine rich necrotrophic effector Tox1(SnTox1) found in Parastagonospora nodorum is a necrotrophic effector that contains 6 cysteine residues, a common feature for some fungal avirulence effectors such as the Avr and ECP effectors from Cladosporium fulvum. The high content of cysteine residues and high stability suggest that SnTox1 may function in the plant apoplastic space which is abundant in plant defense components. Protein sequence analysis indicate that SnTox1 contains a C-terminal chitin binding (CB) like motif. Three-dimensional (3D) structure-based sequence alignment suggested that the putative CB motif in SnTox1 was more similar to those of plant-specific ChtBDs than to Avr4 proteins, which are related to invertebrate ChtBDs. Furthermore, SnTox1 contained all secondary-structure-related residues including the strictly conserved b-strand-forming 'CCS' motif found only in plant-specific ChtBD1 proteins [ , ]. It interacts with the host Snn1 protein conferring susceptibility. Binding of SnTox1 to chitin in the fungal cell wall protects the pathogen from chitinase activity.This entry represents the putative chiting binding-like domain found in SnTox1 from Parastagonospora nodorum. | Name | SnTox1, chitin binding-like domain |
| Short Name | SnTox1_CBL | Type | Domain |
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