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bacteria:t3e:xopd [2020/07/08 16:51] rkoebnik [Further reading] |
bacteria:t3e:xopd [2020/07/08 18:27] (current) rkoebnik [Biological function] |
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Class: XopD (Xanthomonas outer protein D)\\ | Class: XopD (Xanthomonas outer protein D)\\ | ||
- | Family: | + | Family: |
- | Prototype: XopD (// | + | Prototype: XopD (// |
RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
3D structure: [[https:// | 3D structure: [[https:// | ||
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=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
- | XopD is a desumoylating enzyme with strict specificity for its plant small ubiquitin-like modifier (SUMO) substrates (Chosed //et al//., 2007). C-terminus of XopD (amino acids 322–520) shares primary sequence similarity with the C48 family of cysteine peptidases. In the XopD polypeptide, | + | XopD is a desumoylating enzyme with strict specificity for its plant small ubiquitin-like modifier (SUMO) substrates (Chosed //et al//., 2007). C-terminus of XopD (amino acids 322–520) shares primary sequence similarity with the C48 family of cysteine peptidases |
- | Besides C-terminal SUMO protease domain (Chosed | + | Besides C-terminal SUMO protease domain (Hotson |
=== Regulation === | === Regulation === | ||
- | The //xopD// gene expression is induced in a //hrpG//- and // | + | The //xopD// gene expression is induced in a //hrpG//- and // |
=== Phenotypes === | === Phenotypes === | ||
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=== Localization === | === Localization === | ||
- | XopD localizes to subnuclear foci. The N terminus of XopD is required for targeting the effector to the plant nucleus; C-terminal domain encodes a Cys protease that cleaves SUMO-conjugated proteins (Hotson //et al//., 2003; Kim //et al//., 2008)). | + | XopD localizes to subnuclear foci. The N terminus of XopD is required for targeting the effector to the plant nucleus; C-terminal domain encodes a Cys protease that cleaves SUMO-conjugated proteins (Hotson //et al//., 2003; Kim //et al//., 2008). |
=== Enzymatic function === | === Enzymatic function === | ||
- | Peptidase, isopeptidase or desumoylating enzyme (Hotson//et al//., 2003). | + | Peptidase, isopeptidase or desumoylating enzyme (Hotson// et al//., 2003). |
=== Interaction partners === | === Interaction partners === | ||
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===== Further reading ===== | ===== Further reading ===== | ||
- | Canonne J, Marino D, Noël LD, Arechaga I, Pichereaux C, Rossignol M, Roby D, Rivas S (2010). Detection and functional characterization of a 215 amino acid N-terminal extension in the // | + | Canonne J, Marino D, Noël LD, Arechaga I, Pichereaux C, Rossignol M, Roby D, Rivas S (2010). Detection and functional characterization of a 215 amino acid N-terminal extension in the // |
+ | |||
+ | Raffaele S, Rivas S (2013). Regulate and be regulated: integration of defense and other signals by the AtMYB30 transcription factor. Front. Plant Sci. 4: 98. DOI: [[https:// | ||
+ | |||
+ | Tan L, Rong W, Luo H, Chen Y, He C (2014). The // | ||