Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and ...
27-275
3.18e-161
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and are responsible for binding of the toxin to the alpha-2-macroglobulin receptor, with subsequent internalization into endosomes. The domain adopts a thirteen-strand antiparallel beta jelly roll topology, which belongs to the Concanavalin A-like lectins/glucanases fold superfamily.
The actual alignment was detected with superfamily member pfam09101:
Pssm-ID: 286224 Cd Length: 274 Bit Score: 463.06 E-value: 3.18e-161
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
447-618
3.74e-109
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, catalyze the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis.
:
Pssm-ID: 430368 Cd Length: 177 Bit Score: 326.23 E-value: 3.74e-109
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, ...
277-407
3.12e-76
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and are responsible for transmembrane targeting of the toxin, as well as transmembrane translocation of the catalytic domain into the cytoplasmic compartment. A furin cleavage site is present within the domain: cleavage generates a 37 kDa carboxy-terminal fragment, which includes the enzymatic domain, which is then is translocated into the cytoplasm. The domain adopts a helical structure, with six alpha-helices forming a bundle.
:
Pssm-ID: 401151 Cd Length: 142 Bit Score: 239.62 E-value: 3.12e-76
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and ...
27-275
3.18e-161
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and are responsible for binding of the toxin to the alpha-2-macroglobulin receptor, with subsequent internalization into endosomes. The domain adopts a thirteen-strand antiparallel beta jelly roll topology, which belongs to the Concanavalin A-like lectins/glucanases fold superfamily.
Pssm-ID: 286224 Cd Length: 274 Bit Score: 463.06 E-value: 3.18e-161
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
447-618
3.74e-109
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, catalyze the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis.
Pssm-ID: 430368 Cd Length: 177 Bit Score: 326.23 E-value: 3.74e-109
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, ...
277-407
3.12e-76
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and are responsible for transmembrane targeting of the toxin, as well as transmembrane translocation of the catalytic domain into the cytoplasmic compartment. A furin cleavage site is present within the domain: cleavage generates a 37 kDa carboxy-terminal fragment, which includes the enzymatic domain, which is then is translocated into the cytoplasm. The domain adopts a helical structure, with six alpha-helices forming a bundle.
Pssm-ID: 401151 Cd Length: 142 Bit Score: 239.62 E-value: 3.12e-76
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
462-594
1.89e-66
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic Elongation Factor 2, halting protein synthesis. A single molecule of delivered toxin is sufficient to kill a cell. These toxins share mono-ADP-ribosylating activity with a variety of bacterial toxins, such as cholera toxin and pertussis toxin. The structural core is homologous to the poly-ADP ribosylating enzymes such as the PARP enzymes and Tankyrase. Diphtheria toxin is encoded by a lysogenic bacteriophage. Both diphtheria toxin and Pseudomonas aeruginosa exotoxin A are multi-domain proteins. These domains provide a EF2 ADP_ribosylating, receptor-binding, and intracellular trafficking/transmembrane functions .
Pssm-ID: 238716 Cd Length: 147 Bit Score: 214.43 E-value: 1.89e-66
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and ...
27-275
3.18e-161
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and are responsible for binding of the toxin to the alpha-2-macroglobulin receptor, with subsequent internalization into endosomes. The domain adopts a thirteen-strand antiparallel beta jelly roll topology, which belongs to the Concanavalin A-like lectins/glucanases fold superfamily.
Pssm-ID: 286224 Cd Length: 274 Bit Score: 463.06 E-value: 3.18e-161
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
447-618
3.74e-109
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, catalyze the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis.
Pssm-ID: 430368 Cd Length: 177 Bit Score: 326.23 E-value: 3.74e-109
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, ...
277-407
3.12e-76
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and are responsible for transmembrane targeting of the toxin, as well as transmembrane translocation of the catalytic domain into the cytoplasmic compartment. A furin cleavage site is present within the domain: cleavage generates a 37 kDa carboxy-terminal fragment, which includes the enzymatic domain, which is then is translocated into the cytoplasm. The domain adopts a helical structure, with six alpha-helices forming a bundle.
Pssm-ID: 401151 Cd Length: 142 Bit Score: 239.62 E-value: 3.12e-76
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
462-594
1.89e-66
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic Elongation Factor 2, halting protein synthesis. A single molecule of delivered toxin is sufficient to kill a cell. These toxins share mono-ADP-ribosylating activity with a variety of bacterial toxins, such as cholera toxin and pertussis toxin. The structural core is homologous to the poly-ADP ribosylating enzymes such as the PARP enzymes and Tankyrase. Diphtheria toxin is encoded by a lysogenic bacteriophage. Both diphtheria toxin and Pseudomonas aeruginosa exotoxin A are multi-domain proteins. These domains provide a EF2 ADP_ribosylating, receptor-binding, and intracellular trafficking/transmembrane functions .
Pssm-ID: 238716 Cd Length: 147 Bit Score: 214.43 E-value: 1.89e-66
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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