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14  structures 668  species 0  interactions 1214  sequences 223  architectures

Family: CHASE (PF03924)

Summary: CHASE domain

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

CHASE domain Edit Wikipedia article

CHASE
Identifiers
Symbol CHASE
Pfam PF03924
InterPro IPR006189

In molecular biology, the CHASE domain is an extracellular protein domain of 200-230 amino acids, 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 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[edit]

  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. 
  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. 

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

Further reading[edit]

  1. ^ Heyl A, Wulfetange K, Pils B, Nielsen N, Romanov GA, Schmülling T (2007). "Evolutionary proteomics identifies amino acids essential for ligand-binding of the cytokinin receptor CHASE domain.". BMC Evol Biol 7: 62. doi:10.1186/1471-2148-7-62. PMC 1863423. PMID 17439640. 
  2. ^ Pas J, von Grotthuss M, Wyrwicz LS, Rychlewski L, Barciszewski J (2004). "Structure prediction, evolution and ligand interaction of CHASE domain.". FEBS Lett 576 (3): 287–90. doi:10.1016/j.febslet.2004.09.020. PMID 15498549. 
  3. ^ Han QM, Jiang HW, Qi XP, Yu J, Wu P (2004). "A CHASE domain containing protein kinase OsCRL4, represents a new AtCRE1-like gene family in rice.". J Zhejiang Univ Sci 5 (6): 629–33. PMID 15101094. 

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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


External 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

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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
(191)
Full
(1214)
Representative proteomes NCBI
(1200)
Meta
(120)
RP15
(131)
RP35
(283)
RP55
(371)
RP75
(443)
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Format an alignment

  Seed
(191)
Full
(1214)
Representative proteomes NCBI
(1200)
Meta
(120)
RP15
(131)
RP35
(283)
RP55
(371)
RP75
(443)
Alignment:
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Sequence:
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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
(191)
Full
(1214)
Representative proteomes NCBI
(1200)
Meta
(120)
RP15
(131)
RP35
(283)
RP55
(371)
RP75
(443)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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

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Curation and family details

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Curation View help on the curation process

Seed source: [1]
Previous IDs: none
Type: Domain
Author: Yeats C
Number in seed: 191
Number in full: 1214
Average length of the domain: 181.20 aa
Average identity of full alignment: 18 %
Average coverage of the sequence by the domain: 21.82 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 20.5 20.6
Noise cut-off 20.4 20.3
Model length: 193
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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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 seqence.

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