8  structures 681  species 1  interaction 17065  sequences 830  architectures

Family: GGDEF (PF00990)

Summary

GGDEF domain Add an annotation

This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain [1] and has diguanylate cyclase activity [4]. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate.


Literature references

  1. Pei J, Grishin NV; , Proteins 2001;42:210-216.: GGDEF domain is homologous to adenylyl cyclase. PUBMED:11119645

  2. 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

  3. Jenal U; , Curr Opin Microbiol 2004;7:185-191.: Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria?. PUBMED:15063857

  4. Paul R, Weiser S, Amiot NC, Chan C, Schirmer T, Giese B, Jenal U; , Genes Dev 2004;18:715-727.: Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. PUBMED:15075296

  5. Galperin MY; , Environ Microbiol 2004;6:552-567.: Bacterial signal transduction network in a genomic perspective. PUBMED:15142243

  6. Chan C, Paul R, Samoray D, Amiot NC, Giese B, Jenal U, Schirmer T; , Proc Natl Acad Sci U S A 2004;101:17084-17089.: Structural basis of activity and allosteric control of diguanylate cyclase. PUBMED:15569936


InterPro entry IPR000160

This domain appears to be ubiquitous in bacteria and is often linked to a regulatory domain, such as a phosphorylation receiver or oxygen sensing domain. Its function is to synthesize cyclic di-GMP, which is used as an intracellular signalling molecule in a wide variety of bacteria PUBMED:15075296,PUBMED:15716451. Enzymatic activity can be strongly influenced by the adjacent domains. Processes regulated by this domain include exopolysaccharide synthesis, biofilm formation, motility and cell differentiation.

Structural studies of PleD from Caulobacter crescentus show that this domain forms a five-stranded beta sheet surrounded by helices, similar to the catalytic core of adenylate cyclase PUBMED:15569936.

Clan

This family is a member of clan Nucleot_cyclase (CL0276), which contains the following 3 members:

GGDEF GGDN Guanylate_cyc

External database links

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 HMMER2.

Pfam alignments:

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. 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: Pfam-B_112 (release 3.0)
Previous IDs: DUF9;
Type: Domain
Author: Bateman A
Number in seed: 49
Number in full: 17065
Average length of the domain: 153.60 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 26.61 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.0 21.0
Noise cut-off 20.9 20.9
Model length: 161
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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

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Interactions

There is 1 interaction for this family. More...

Response_reg

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 MSD 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 GGDEF domain has been found.

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