Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and ...
27-275
8.17e-162
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: 464.60 E-value: 8.17e-162
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
447-618
6.52e-108
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.
The actual alignment was detected with superfamily member pfam09009:
Pssm-ID: 444809 Cd Length: 177 Bit Score: 322.76 E-value: 6.52e-108
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, ...
277-407
1.00e-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: 241.16 E-value: 1.00e-76
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and ...
27-275
8.17e-162
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: 464.60 E-value: 8.17e-162
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
447-618
6.52e-108
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: 322.76 E-value: 6.52e-108
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, ...
277-407
1.00e-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: 241.16 E-value: 1.00e-76
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
462-594
3.34e-65
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: 210.97 E-value: 3.34e-65
Exotoxin A binding; Members of this family are found in Pseudomonas aeruginosa exotoxin A, and ...
27-275
8.17e-162
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: 464.60 E-value: 8.17e-162
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
447-618
6.52e-108
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: 322.76 E-value: 6.52e-108
Exotoxin A, targeting; Members of this family are found in Pseudomonas aeruginosa exotoxin A, ...
277-407
1.00e-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: 241.16 E-value: 1.00e-76
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
462-594
3.34e-65
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: 210.97 E-value: 3.34e-65
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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(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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