Summary: Elicitin
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This is the Wikipedia entry entitled "Elicitin". More...
Elicitin Edit Wikipedia article
| beta-cinnamomin in complex with ergosterol | |||||||||
| Identifiers | |||||||||
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| Symbol | Elicitin | ||||||||
| Pfam | PF00964 | ||||||||
| InterPro | IPR002200 | ||||||||
| SCOP | 1beo | ||||||||
| SUPERFAMILY | 1beo | ||||||||
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In molecular biology, elicitins are a family of small, highly-conserved proteins secreted by phytopathogenic microorganisms belonging to the Phytophthora and Pythium species.[1] They are toxic proteins responsible for inducing a necrotic and systemic hypersensitive response in plants from the Solanaceae and Cruciferae families. Leaf necrosis provides immediate control of fungal invasion and induces systemic acquired resistance; both responses mediate basic protection against subsequent pathogen inoculation.
Members of this family share a high level of sequence similarity, but they differ in net charge, dividing them into two classes: alpha and beta.[1] Alpha-elicitins are highly acidic, with a valine residue at position 13, whereas beta-elicitins are basic, with a lysine at the same position. Residue 13 is known to be involved in the control of necrosis and, being exposed, is thought to be involved in ligand/receptor binding.[2] Phenotypically, the two classes can be distinguished by their necrotic properties: beta-elicitins are 100-fold more toxic and provide better subsequent protection[1]
[edit] References
- ^ a b c Yu LM (May 1995). "Elicitins from Phytophthora and basic resistance in tobacco". Proc. Natl. Acad. Sci. U.S.A. 92 (10): 4088–94. DOI:10.1073/pnas.92.10.4088. PMC 41891. PMID 7753775. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41891.
- ^ Fefeu S, Bouaziz S, Huet JC, Pernollet JC, Guittet E (November 1997). "Three-dimensional solution structure of beta cryptogein, a beta elicitin secreted by a phytopathogenic fungus Phytophthora cryptogea". Protein Sci. 6 (11): 2279–84. DOI:10.1002/pro.5560061101. PMC 2143581. PMID 9385630. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2143581.
This article incorporates text from the public domain Pfam and InterPro IPR002200
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.
Elicitin Provide feedback
Elicitins form a novel class of plant necrotic proteins which are secreted by Phytophthora and Pythium fungi, parasites of many economically important crops. These proteins induce leaf necrosis in infected plants and elicit an incompatible hypersensitive-like reaction, leading to the development of a systemic acquired resistance against a range of fungal and bacterial plant pathogens [1].
Literature references
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Boissy G, de La Fortelle E, Kahn R, Huet JC, Bricogne G, Pernollet JC, Brunie S; , Structure 1996;4:1429-1439.: Crystal structure of a fungal elicitor secreted by Phytophthora cryptogea, a member of a novel class of plant necrotic proteins. PUBMED:8994969 EPMC:8994969
External database links
| PANDIT: | PF00964 |
| Pseudofam: | PF00964 |
| SCOP: | 1beo |
| SYSTERS: | Elicitin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002200
Elicitins are a family of small, highly-conserved proteins secreted by phytopathogenic fungi belonging to the phytophthora species [PUBMED:7753775, PUBMED:]. They are toxic proteins reponsible for inducing a necrotic and systemic hypersensitive response in plants from the solanaceae and cruciferae families. Leaf necrosis provides immediate control of fungal invasion and induces systemic acquired resistance; both responses mediate basic protection against subsequent pathogen inoculation.
Members of this family share a high level of sequence similarity, but they differ in net charge, dividing them into two classes: alpha and beta [PUBMED:7753775, PUBMED:]. Alpha-elicitins are highly acidic, with a valine residue at position 13, whereas beta-elicitins are basic, with a lysine at the same position. Residue 13 is known to be involved in the control of necrosis and, being exposed, is thought to be involved in ligand/receptor binding [PUBMED:, PUBMED:9385630]. Phenotypically, the two classes can be distinguished by their necrotic properties: beta-elicitins are 100-fold more toxic and provide better subsequent protection [PUBMED:7753775, PUBMED:].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | extracellular region (GO:0005576) |
| Biological process | defense response (GO:0006952) |
| pathogenesis (GO:0009405) |
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
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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 (87) |
Full (406) |
Representative proteomes | NCBI (325) |
Meta (0) |
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| RP15 (59) |
RP35 (101) |
RP55 (173) |
RP75 (173) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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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 (87) |
Full (406) |
Representative proteomes | NCBI (325) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (59) |
RP35 (101) |
RP55 (173) |
RP75 (173) |
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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.
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
| Seed source: | Sarah Teichmann |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 87 |
| Number in full: | 406 |
| Average length of the domain: | 89.40 aa |
| Average identity of full alignment: | 32 % |
| Average coverage of the sequence by the domain: | 49.01 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 90 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
ElicitinStructures
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 Elicitin domain has been found. There are 16 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence