62  structures 46  species 1  interaction 346  sequences 1  architecture

Family: Toxin_3 (PF00537)

Summary

Scorpion toxin-like domain Add an annotation

This family contains both neurotoxins and plant defensins. The mustard trypsin inhibitor, MTI-2, is plant defensin. It is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for Lepidopteran insects, but has low activity against aphids [1]. Brazzein is plant defensin-like protein. It is pH-stable, heat-stable and intensely sweet protein [2]. The scorpion toxin (a neurotoxin) binds to sodium channels and inhibits the activation mechanisms of the channels, thereby blocking neuronal transmission. Scorpion toxins bind to sodium channels and inhibit the activation mechanisms of the channels, thereby blocking neuronal transmission


Literature references

  1. Ceci LR, Volpicella M, Rahbe Y, Gallerani R, Beekwilder J, Jongsma MA; , Plant J 2003;33:557-566.: Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids. PUBMED:12581313

  2. Assadi-Porter FM, Aceti DJ, Markley JL; , Arch Biochem Biophys 2000;376:259-265.: Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein. PUBMED:10775411


InterPro entry IPR002061

Scorpion toxins, which may be mammal or insect specific, bind to sodium channels, inhibiting the inactivation of activated channels and blocking neuronal transmission. The complete covalent structure of the toxins has been deduced: it comprises around 66 amino acid residues and is cross- linked by 4 disulphide bridges PUBMED:2311768, PUBMED:6845379. An anti-epilepsy peptide isolated from scorpion venom PUBMED:2930463 shows similarity to both scorpion neurotoxins and anti-insect toxins.

This family also contains a group of proteinase inhibitors from Arabidopsis thaliana and Brassica spp., which belong to MEROPS inhibitor family I18, clan I-. The Brassica napus (Oil seed rape) and Sinapis alba (White mustard) inhibitors PUBMED:8143882, PUBMED:1451776, inhibit the catalytic activity of bovine beta-trypsin and bovine alpha-chymotrypsin, which belong to MEROPS peptidase family S1 () PUBMED:14705960.

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_5

Gene Ontology

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

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...

View options

Alignment:
Viewer:  

Formatting options

Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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.

Pfam alignments:
Full length sequences

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.

Pfam alignments:

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 View help on the curation process

Seed source: Pfam-B_8170 (release 8.0)
Previous IDs: toxin_3;
Type: Domain
Author: Bateman A, Moxon SJ, Finn RD
Number in seed: 35
Number in full: 346
Average length of the domain: 53.10 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 70.33 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.5 21.5
Trusted cut-off 21.5 21.5
Noise cut-off 20.9 21.4
Model length: 54
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Interactions

There is 1 interaction for this family. More...

Toxin_3

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_3 domain has been found.

Loading structure mapping...