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15  structures 1591  species 2  interactions 17337  sequences 837  architectures

Family: EAL (PF00563)

Summary: EAL domain

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This is the Wikipedia entry entitled "EAL domain". More...

EAL domain Edit Wikipedia article

EAL domain
PDB 2bas EBI.jpg
crystal structure of the bacillus subtilis ykui protein, with an eal domain.
Identifiers
Symbol EAL
Pfam PF00563
InterPro IPR001633
CDD cd01948

In molecular biology, the EAL domain is a conserved protein domain. It is found in diverse bacterial signalling proteins. It is named EAL after its conserved residues. The EAL domain may function as a diguanylate phosphodiesterase.[1] The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.

[edit] References

  1. ^ Galperin MY, Nikolskaya AN, Koonin EV (September 2001). "Novel domains of the prokaryotic two-component signal transduction systems". FEMS Microbiol. Lett. 203 (1): 11–21. doi:10.1016/S0378-1097(01)00326-3. PMID 11557134. 

This article incorporates text from the public domain Pfam and InterPro IPR001633

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.

EAL domain

This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function [1]. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site [1].

Literature references

  1. Galperin MY, Nikolskaya AN, Koonin EV; , FEMS Microbiol Lett 2001;203:11-21.: Novel domains of the prokaryotic two-component signal transduction systems. PUBMED:11557134



External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001633

This domain is found in diverse bacterial signalling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function [PUBMED:11557134]. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site. It often but not always occurs along with INTERPRO and INTERPRO domains that are also found in many signalling proteins.

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

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...

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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 HMMER3.

Pfam alignments:

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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: Alignment kindly provided by SMART
Previous IDs: DUF2;
Type: Domain
Author: SMART
Number in seed: 138
Number in full: 17337
Average length of the domain: 228.60 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 36.23 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.8 20.7
Noise cut-off 20.5 20.6
Model length: 236
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Interactions

There are 2 interactions for this family. More...

EAL YkuI_C

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 EAL domain has been found. There are 15 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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