Summary: Gamma-thionin family
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Gamma thionin Edit Wikipedia article
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Gamma-thionin family Provide feedback
No Pfam abstract.
Internal database links
|SCOOP:||Toxin_2 Toxin_3 Defensin_2 SLR1-BP|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008176
The following small plant proteins are evolutionary related:
- Gamma-thionins from Triticum aestivum (Wheat) endosperm (gamma-purothionins) and gamma-hordothionins from Hordeum vulgare(Barley) are toxic to animal cells and inhibit protein synthesis in cell free systems [PUBMED:8380707].
- A flower-specific thionin (FST) from Nicotiana tabacum (Common Tobacco)[PUBMED:1495489].
- Antifungal proteins (AFP) from the seeds of Brassicaceae species such as radish, mustard, turnip and Arabidopsis thaliana (Thale Cress)[PUBMED:8422949].
- Inhibitors of insect alpha-amylases from sorghum [PUBMED:1995329].
- Probable protease inhibitor P322 from Solanum tuberosum (Potato).
- A germination-related protein from Vigna unguiculata (Cowpea) [PUBMED:2103443].
- Anther-specific protein SF18 from sunflower. SF18 is a protein that contains a gamma-thionin domain at its N terminus and a proline-rich C-terminal domain.
- Glycine max (Soybean) sulphur-rich protein SE60 [PUBMED:8278516].
- Vicia faba (Broad bean) antibacterial peptides fabatin-1 and -2.
In their mature form, these proteins generally consist of about 45 to 50 amino-acid residues. As shown in the following schematic representation, these peptides contain eight conserved cysteines involved in disulphide bonds.
+-------------------------------------------+ | +-------------------+ | | | | | xxCxxxxxxxxxxCxxxxxCxxxCxxxxxxxxxCxxxxxxCxCxxxC | | | | +---|----------------+ | +------------------+ 'C': conserved cysteine involved in a disulphide bond.
The folded structure of Gamma-purothionin is characterised by a well-defined 3-stranded anti-parallel beta-sheet and a short alpha-helix [PUBMED:8380707]. Three disulphide bridges are located in the hydrophobic core between the helix and sheet, forming a cysteine-stabilised alpha-helical motif. This structure differs from that of the plant alpha- and beta- thionins, but is analogous to scorpion toxins and insect defensins.
|Biological process||defense response (GO:0006952)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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This clan includes a number of toxin families that share the knottin structure. These families come from scorpions, plants and arthropods.
The clan contains the following 13 members:BmKX Defensin_2 Defensin_like Gamma-thionin SCRL SLR1-BP Toxin_17 Toxin_2 Toxin_3 Toxin_37 Toxin_38 Toxin_5 Toxin_6
We make a range of alignments for each Pfam-A family:
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Key: available, not generated, — not available.
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Curation and family details
|Number in seed:||25|
|Number in full:||452|
|Average length of the domain:||47.50 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||56.40 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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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 Gamma-thionin domain has been found. There are 37 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 seqence.
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