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14  structures 1723  species 1  interaction 3336  sequences 598  architectures

Family: CHASE (PF03924)

Summary: CHASE domain

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CHASE domain Edit Wikipedia article

CHASE
Identifiers
Symbol CHASE
Pfam PF03924
InterPro IPR006189

The CHASE domain is an extracellular protein domain, which is found in transmembrane receptor from bacteria, lower eukaryotes and plants. It has been named CHASE (Cyclases/Histidine kinases Associated Sensory Extracellular) because of its presence in diverse receptor-like proteins with histidine kinase and nucleotide cyclase domains. The CHASE domain is 200-230 amino acids long and always occurs N-terminally in extracellular or periplasmic locations, followed by an intracellular tail housing diverse enzymatic signalling domains such as histidine kinase, adenyl cyclase, GGDEF-type nucleotide cyclase and EAL-type phosphodiesterase domains, as well as non-enzymatic domains such PAS, GAF, phosphohistidine and response regulatory domains. The CHASE domain is predicted to bind diverse low molecular weight ligands, such as the cytokinin-like adenine derivatives or peptides, and mediate signal transduction through the respective receptors.[1][2]

The CHASE domain has a predicted alpha+beta fold, with two extended alpha helices on both boundaries and two central alpha helices separated by beta sheets. The termini are less conserved compared with the central part of the domain, which shows strongly conserved motif.

References

  1. ^ Anantharaman V, Aravind L (October 2001). "The CHASE domain: a predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors". Trends Biochem. Sci. 26 (10): 579–82. PMID 11590000. doi:10.1016/s0968-0004(01)01968-5. 
  2. ^ Mougel C, Zhulin IB (October 2001). "CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants". Trends Biochem. Sci. 26 (10): 582–4. PMID 11590001. doi:10.1016/s0968-0004(01)01969-7. 

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR006189

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.

CHASE domain Provide feedback

This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases [1,2]. Predicted to be a ligand binding domain [1].

Literature references

  1. Anantharaman V, Aravind L; , Trends Biochem Sci 2001;26:579-582.: The CHASE domain: a predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors. PUBMED:11590000 EPMC:11590000

  2. Mougel C, Zhulin IB; , Trends Biochem Sci 2001;26:582-584.: CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants. PUBMED:11590001 EPMC:11590001


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006189

The CHASE domain is an extracellular domain of 200-230 amino acids, which is found in transmembrane receptors from bacteria, lower eukaryotes and plants. It has been named CHASE (Cyclases/Histidine kinases Associated Sensory Extracellular) because of its presence in diverse receptor-like proteins with histidine kinase and nucleotide cyclase domains. The CHASE domain always occurs N-terminally in extracellular or periplasmic locations, followed by an intracellular tail housing diverse enzymatic signalling domains such as histidine kinase (INTERPRO), adenyl cyclase, GGDEF-type nucleotide cyclase and EAL-type phosphodiesterase domains, as well as non-enzymatic domains such PAS (INTERPRO), GAF (INTERPRO), phosphohistidine and response regulatory domains. The CHASE domain is predicted to bind diverse low molecular weight ligands, such as the cytokinin-like adenine derivatives or peptides, and mediate signal transduction through the respective receptors [PUBMED:11590001, PUBMED:11590000].

The CHASE domain has a predicted alpha+beta fold, with two extended alpha helices on both boundaries and two central alpha helices separated by beta sheets. The termini are less conserved compared with the central part of the domain, which shows strongly conserved motifs.

Domain organisation

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

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Pfam Clan

This family is a member of clan Cache (CL0165), which has the following description:

The Cache domain an extracellular domain that is thought to have a role in small-molecule recognition in a wide range of proteins, including the animal Ca(2+)-channel subunits and a class of prokaryotic chemotaxis receptors [1]. It is homologous to, but sufficiently different from the most common intracellular sensor module, the PAS domain. Furthermore, it is suggested that it might have originated from a simpler intracellular PAS/GAF ancestor as a benefit of extracellular sensing [2].

The clan contains the following 24 members:

2CSK_N Cache_3-Cache_2 CHASE CHASE4 CHASE7 CHASE8 dCache_1 dCache_2 dCache_3 Diacid_rec DUF2222 DUF4153 DUF4173 GAPES1 LuxQ-periplasm PhoQ_Sensor sCache_2 sCache_3_2 sCache_3_3 sCache_like SMP_2 Stimulus_sens_1 VGCC_alpha2 YkuI_C

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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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
(200)
Full
(3336)
Representative proteomes UniProt
(8404)
NCBI
(14414)
Meta
(112)
RP15
(723)
RP35
(2141)
RP55
(3345)
RP75
(4742)
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Key: ✓ available, x not generated, not available.

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  Seed
(200)
Full
(3336)
Representative proteomes UniProt
(8404)
NCBI
(14414)
Meta
(112)
RP15
(723)
RP35
(2141)
RP55
(3345)
RP75
(4742)
Alignment:
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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
(200)
Full
(3336)
Representative proteomes UniProt
(8404)
NCBI
(14414)
Meta
(112)
RP15
(723)
RP35
(2141)
RP55
(3345)
RP75
(4742)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   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.

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.

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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: [1]
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Yeats C
Number in seed: 200
Number in full: 3336
Average length of the domain: 175.40 aa
Average identity of full alignment: 18 %
Average coverage of the sequence by the domain: 20.40 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.5 21.5
Trusted cut-off 21.5 21.5
Noise cut-off 21.4 21.4
Model length: 188
Family (HMM) version: 13
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 is 1 interaction for this family. More...

CHASE

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 CHASE domain has been found. There are 14 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 sequence.

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