TraB/GumN family protein similar to Escherichia coli protein YbaP and eukaryotic metalloprotease TIKI, which acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
39-302
6.02e-82
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.
Pssm-ID: 350614 Cd Length: 259 Bit Score: 248.37 E-value: 6.02e-82
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
38-304
2.50e-78
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.
Pssm-ID: 426534 Cd Length: 262 Bit Score: 239.18 E-value: 2.50e-78
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
39-302
6.02e-82
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.
Pssm-ID: 350614 Cd Length: 259 Bit Score: 248.37 E-value: 6.02e-82
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
38-304
2.50e-78
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.
Pssm-ID: 426534 Cd Length: 262 Bit Score: 239.18 E-value: 2.50e-78
poorly characterized family of proteins related to gumN pathogenicity factor of Xanthomonas; ...
39-303
8.43e-10
poorly characterized family of proteins related to gumN pathogenicity factor of Xanthomonas; GumN, a poorly characterized protein, is part of the large gum cluster of pathogenicity factors of the plant pathogen Xanthomonas. Except for GumN, the gum cluster is conserved, and proteins of this operon are involved in the production of xanthan, an extracellular polysaccharide that promotes plant disease. Xanthomonas campestri is responsible for 'black rot' disease in certain crop plants. GumN has sequence similarity to the Tiki/TraB protease family, but lacks the typical conserved residues of the active site.
Pssm-ID: 350613 Cd Length: 286 Bit Score: 58.40 E-value: 8.43e-10
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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