Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
17  structures 132  species 0  interactions 545  sequences 2  architectures

Family: Gamma-thionin (PF00304)

Summary: Gamma-thionin family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Gamma thionin". More...

Gamma thionin Edit Wikipedia article

Plant defensins
1ayj.gif
Antifungal protein 1
Identifiers
Symbol Gamma-thionin
Pfam PF00304
Pfam clan CL0054
InterPro IPR008176
PROSITE PDOC00725
SCOP 1gps
SUPERFAMILY 1gps
OPM superfamily 61
OPM protein 1jkz
CDD cd00107

Gamma-thionins (also known as plant defensins) are small evolutionarily related proteins of plants that serve to defend them against parasites.

The following plant proteins belong to this family:

  • 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.[1]
  • A flower-specific thionin (FST) from Nicotiana tabacum (Common Tobacco).[2]
  • Antifungal proteins (AFP) from the seeds of Brassicaceae species such as radish, mustard, turnip and Arabidopsis thaliana (Thale Cress).[3]
  • Inhibitors of insect alpha-amylases from sorghum.[4]
  • Probable protease inhibitor P322 from Solanum tuberosum (Potato).
  • A germination-related protein from Vigna unguiculata (Cowpea).[5]
  • 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) sulfur-rich protein SE60.[6]
  • 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 disulfide bonds.

         +-------------------------------------------+
         |          +-------------------+            |
         |          |                   |            |
       xxCxxxxxxxxxxCxxxxxCxxxCxxxxxxxxxCxxxxxxCxCxxxC
                          |   |                | |
                          +---|----------------+ |
                              +------------------+

'C': conserved cysteine involved in a disulfide bond.

The folded structure of Gamma-purothionin is characterised by a well-defined 3-stranded anti-parallel beta-sheet and a short alpha-helix.[1] Three disulfide 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.

Databases[edit]

A database for antimicrobial peptides, including defensins is available: PhytAMP (http://phytamp.pfba-lab.org).[7]

References[edit]

  1. ^ a b Bruix M, Jime nez MA, Santoro J, Gonzalez C, Colilla FJ, Mendez E, Rico M (1993). "Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins". Biochemistry 32 (2): 715–724. doi:10.1021/bi00053a041. PMID 8380707. 
  2. ^ Gu Q, Kawata EE, Cheung AY, Morse MJ, Wu HM (1992). "A flower-specific cDNA encoding a novel thionin in tobacco". Mol. Gen. Genet. 234 (1): 89–96. PMID 1495489. 
  3. ^ Osborn RW, Torrekens S, Vanderleyden J, Broekaert WF, Cammue BP, Terras FR, Van Leuven F (1993). "A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species". FEBS Lett. 316 (3): 233–240. doi:10.1016/0014-5793(93)81299-F. PMID 8422949. 
  4. ^ Richardson M, Bloch Jr C (1991). "A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins". FEBS Lett. 279 (1): 101–104. doi:10.1016/0014-5793(91)80261-Z. PMID 1995329. 
  5. ^ Ishibashi N, Yamauchi D, Minamikawa T (1990). "Stored mRNA in cotyledons of Vigna unguiculata seeds: nucleotide sequence of cloned cDNA for a stored mRNA and induction of its synthesis by precocious germination". Plant Mol. Biol. 15 (1): 59–64. doi:10.1007/BF00017724. PMID 2103443. 
  6. ^ Choi Y, Choi YD, Lee JS (1993). "Nucleot ide sequence of a cDNA encoding a low molecular weight sulfur-rich protein in soybean seeds". Plant Physiol. 101 (2): 699–700. doi:10.1104/pp.101.2.699. PMC 160625. PMID 8278516. 
  7. ^ Hammami R, Ben Hamida J, Vergoten G, Fliss I, (2008). "PhytAMP: a database dadicated to plant antimicrobial peptides.". Nucleic Acid Research 37 (Database issue): D963. doi:10.1093/nar/gkn655. PMC 2686510. PMID 18836196. 

Subfamilies[edit]

This article incorporates text from the public domain Pfam and InterPro IPR008176

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Gamma-thionin family Provide feedback

No Pfam abstract.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008176

The following small plant proteins are evolutionary related:

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.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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

Loading domain graphics...

Pfam Clan

This family is a member of clan Knottin_1 (CL0054), which has the following description:

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 11 members:

Defensin_2 DUF2667 Gamma-thionin SCRL SLR1-BP Toxin_17 Toxin_2 Toxin_3 Toxin_37 Toxin_38 Toxin_5

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(50)
Full
(545)
Representative proteomes NCBI
(592)
Meta
(0)
RP15
(27)
RP35
(58)
RP55
(87)
RP75
(121)
Jalview View  View  View  View  View  View  View   
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(50)
Full
(545)
Representative proteomes NCBI
(592)
Meta
(0)
RP15
(27)
RP35
(58)
RP55
(87)
RP75
(121)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(50)
Full
(545)
Representative proteomes NCBI
(592)
Meta
(0)
RP15
(27)
RP35
(58)
RP55
(87)
RP75
(121)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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 HMMER3.

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'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.

Note: You can also download the data file for the tree.

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: Prosite
Previous IDs: none
Type: Domain
Author: Finn RD
Number in seed: 50
Number in full: 545
Average length of the domain: 46.80 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 59.18 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.7
Noise cut-off 20.6 20.6
Model length: 47
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

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

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

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 Gamma-thionin domain has been found. There are 17 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.

Loading structure mapping...