Summary: Clostridium neurotoxin, Translocation domain
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Clostridium neurotoxin, Translocation domain Provide feedback
The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (PF01742), the central translocation domains and two receptor binding domains [1]. Subsequent to cell surface binding and receptor mediated endocytosis of the neurotoxin, an acid induced conformational change in the neurotoxin translocation domain is believed to allow the domain to penetrate the endosome and from a pore, thereby facilitating the passage of the catalytic domain across the membrane into the cytosol [1]. The structure of the translocation reveals a pair of helices that are 105 Angstroms long and is structurally distinct from other pore forming toxins [1].
Literature references
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Lacy DB, Tepp W, Cohen AC, DasGupta BR, Stevens RC; , Nat Struct Biol 1998;5:898-902.: Crystal structure of botulinum neurotoxin type A and implications for toxicity. PUBMED:9783750 EPMC:9783750
This tab holds annotation information from the InterPro database.
InterPro entry IPR012500
The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein: a N-terminal catalytic domain ( INTERPRO ), a central translocation domain and two receptor binding domains [ PUBMED:9783750 ]. Subsequent to cell surface binding and receptor mediated endocytosis of the neurotoxin, an acid induced conformational change in the neurotoxin translocation domain is believed to allow the domain to penetrate the endosome and from a pore, thereby facilitating the passage of the catalytic domain across the membrane into the cytosol [ PUBMED:9783750 ]. The structure of the translocation reveals a pair of helices that are 105 Angstroms long and is structurally distinct from other pore forming toxins [ PUBMED:9783750 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | protein transmembrane transporter activity (GO:0008320) |
Biological process | negative regulation of neurotransmitter secretion (GO:0046929) |
Domain organisation
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Alignments
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Seed (2) |
Full (8) |
Representative proteomes | UniProt (207) |
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RP15 (1) |
RP35 (5) |
RP55 (8) |
RP75 (12) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (2) |
Full (8) |
Representative proteomes | UniProt (207) |
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RP15 (1) |
RP35 (5) |
RP55 (8) |
RP75 (12) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_4943 (release 15.0) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 2 |
Number in full: | 8 |
Average length of the domain: | 292.6 aa |
Average identity of full alignment: | 38 % |
Average coverage of the sequence by the domain: | 25.71 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 322 | ||||||||||||
Family (HMM) version: | 15 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Toxin_trans domain has been found. There are 71 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
Protein | Predicted structure | External Information |
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P04958 | View 3D Structure | Click here |
P0DPI1 | View 3D Structure | Click here |