SUPERFAMILY 1.75 HMM library and genome assignments server


Fungal elicitin superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All alpha proteins [ 46456] (284)
Fold:   Fungal elicitin [ 48646]
Superfamily:   Fungal elicitin [ 48647]
Families:   Fungal elicitin [ 48648] (2)


Superfamily statistics
Genomes (6) Uniprot 2013_05 PDB chains (SCOP 1.75)
Domains 227 436 4
Proteins 216 426 4


Functional annotation
General category coiled coil
Detailed category This is a complex coiled arrangement. The details of which will appear on this page shortly (some coiled coil details are being checked before they are included on the site). If you want to see examples of the states please click here here. If you require further details urgently please contact Owen Rackham

Document:
Function annotation of SCOP domain superfamilies

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Cellular componentSecreted0Moderately InformativeDirect
DomainSignal1.201e-05Least InformativeDirect
Post-translational modificationDisulfide bond0Least InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR002200 SSF48647 Protein matches
Abstract

Elicitins are a family of small, highly-conserved proteins secreted by phytopathogenic fungi belonging to the phytophthora species [PubMed7753775]. 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 [PubMed7753775]. 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 [, PubMed9385630]. Phenotypically, the two classes can be distinguished by their necrotic properties: beta-elicitins are 100-fold more toxic and provide better subsequent protection [PubMed7753775].


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

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Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 2 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Fungal elicitin domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 2 hidden Markov models representing the Fungal elicitin superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · UniProtKB KeyWords (KW) · Internal database links ]