Summary
Ergtoxin family
This family consists of ergtoxin peptides which are toxins secreted by the scorpions. The ergtoxins are capable of blocking the function of K+ channels. More than 100 ergtoxins have been found from scorpion venoms and they have been classified into three subfamilies according to their primary structures [1].
Literature references
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Frenal K, Xu CQ, Wolff N, Wecker K, Gurrola GB, Zhu SY, Chi CW, Possani LD, Tytgat J, Delepierre M; , Proteins 2004;56:367-375.: Exploring structural features of the interaction between the scorpion toxinCnErg1 and ERG K+ channels. PUBMED:15211519
InterPro entry IPR012622
The Ergtoxin (ErgTx) family is a class of peptides from scorpion venom that specifically block ERG (ether-a-go-go-related gene) K+ channels of the nerve, heart and endocrine cells PUBMED:11023354, PUBMED:12650941, PUBMED:12459475.
Peptides of the ErgTx family have from 42 to 47 amino acid residues cross-linked by four disulphide bridges. The four disulphide bridges have been assigned as C1-C4, C2-C6, C3-C7 and C5-C8 (see the schematic representation below) PUBMED:11023354. ErgTxs consist of a triple-stranded beta-sheet and an alpha-helix, as is typical of K+ channel scorpion toxins. There is a large hydrophobic patch on the surface of the toxin, surrounding a central lysine residue located near the beta-hairpin loop between the second and third strands of the beta-sheet. It has been postulated that this hydrophobic patch is likely to form part of the binding surface of the toxin PUBMED:12650941. Peptides of the ErgTx family possess a Knottin scaffold (see http://knottin.cbs.cnrs.fr).
Some proteins known to belong to the ErgTx family are listed below:
- ErgTx1, ErgTx2 and ErgTx3 from Centruroides elegans (Bark scorpion).
- ErgTx1, ErgTx2, ErgTx3 and ErgTx4 from Centruroides exilicauda (Bark scorpion).
- ErgTx1, ErgTx2 and ErgTx3 from Centruroides gracilis (Slenderbrown scorpion) (Florida bark scorpion).
- ErgTx1, ErgTx2, ErgTx3 and ErgTx4 from Centruroides limpidus limpidus (Mexican scorpion).
- ErgTx1, ErgTx2, ErgTx3, ErgTx4, ErgTx5 and gamma-KTx 4.12 from Centruroides sculpturatus (Bark scorpion).
- ErgTx, ErgTx2, ErgTx3, ErgTx4 and ErgTx5 from Centruroides noxius (Mexican scorpion).
Clan
This family is a member of clan Knottin_1 (CL0054), which contains the following 10 members:
Defensin_2 DUF2667 Gamma-thionin SCRL SLR1-BP Toxin_17 Toxin_2 Toxin_3 Toxin_37 Toxin_5Gene Ontology
| Cellular component | extracellular region (GO:0005576) |
| Molecular function | potassium channel inhibitor activity (GO:0019870) |
| Biological process | pathogenesis (GO:0009405) |
External database links
| PANDIT: | PF08086 |
| SYSTERS: | Toxin_17 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
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Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | Short protein clustering |
| Previous IDs: | none |
| Type: | Family |
| Author: | Lee SC |
| Number in seed: | 4 |
| Number in full: | 27 |
| Average length of the domain: | 41.00 aa |
| Average identity of full alignment: | 79 % |
| Average coverage of the sequence by the domain: | 93.81 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 41 | ||||||||||||
| Family (HMM) version: | 4 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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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_17 domain has been found.
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