Summary: CBS domain
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This is the Wikipedia entry entitled "CBS domain". More...
CBS domain Edit Wikipedia article
The CBS domain is a protein domain that is found in a range of proteins all species. The CBS domain was first identified as a conserved sequence region in 1997.[1][2] CBS domains are found in a wide variety of proteins such as Cystathionine beta synthase, Inosine monophosphate dehydrogenase and voltage gated chloride channels. It has been shown that CBS domains bind to adenosyl groups in molecules such as AMP and ATP. Upon binding these different molecules the CBS domains regulate the activity of associated enzymatic domains.[3]
References
- ^ Bateman A (1997). "The structure of a domain common to archaebacteria and the homocystinuria disease protein". Trends Biochem. Sci. 22 (1): 12–3. PMID 9020585.
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ignored (help) - ^ Ponting CP (1997). "CBS domains in CIC chloride channels implicated in myotonia and nephrolithiasis (kidney stones)". J. Mol. Med. 75 (3): 160–3. PMID 9106071.
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ignored (help) - ^ Scott JW, Hawley SA, Green KA; et al. (2004). "CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations". J. Clin. Invest. 113 (2): 274–84. doi:10.1172/JCI19874. PMC 311435. PMID 14722619.
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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.
CBS domain Provide feedback
CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet [4]. CBS domain pairs from AMPK bind AMP or ATP [5]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [5].
Literature references
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Bateman A; , Trends Biochem Sci 1997;22:12-13.: The structure of a domain common to archaebacteria and the homocystinuria disease protein. PUBMED:9020585 EPMC:9020585
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Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR; , Biochemistry 1999;38:4691-4700.: Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. PUBMED:10200156 EPMC:10200156
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Ponting CP; , J Mol Med 1997;75:160-163.: CBS domains in ClC chloride channels implicated in myotonia and nephrolithiasis (kidney stones). PUBMED:9106071 EPMC:9106071
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Janosik M, Kery V, Gaustadnes M, Maclean KN, Kraus JP , Biochemistry 2001;40:10625-10633.: Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. PUBMED:11524006 EPMC:11524006
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Scott JW, Hawley SA, Green KA, Anis M, Stewart G, Scullion GA, Norman DG, Hardie DG; , J Clin Invest 2004;113:274-284.: CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. PUBMED:14722619 EPMC:14722619
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Kemp BE; , J Clin Invest 2004;113:182-184.: Bateman domains and adenosine derivatives form a binding contract. PUBMED:14722609 EPMC:14722609
Internal database links
SCOOP: | AAA_15 AAA_16 DHH FMN_dh His_biosynth IMPDH NMO |
Similarity to PfamA using HHSearch: | IMPDH IMPDH |
External database links
HOMSTRAD: | CBS |
MIM: | 236200 |
SCOP: | 1zfj |
SMART: | CBS |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000644
CBS domains are small intracellular modules that pair together to form a stable globular domain [ PUBMED:10200156 ]. Pairs of these domains have been termed a Bateman domain [ PUBMED:14722609 ]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [ PUBMED:14722619 ]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in cystathionine-beta synthase is involved in regulation by S-AdoMet [ PUBMED:11524006 ]. CBS domain pairs from AMPK bind AMP or ATP [ PUBMED:14722619 ]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [ PUBMED:14722619 ].
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
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 and the UniProtKB 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 (840) |
Full (185434) |
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RP15 (25040) |
RP35 (85562) |
RP55 (181009) |
RP75 (301618) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (840) |
Full (185434) |
Representative proteomes | UniProt (735709) |
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RP15 (25040) |
RP35 (85562) |
RP55 (181009) |
RP75 (301618) |
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Raw Stockholm | |||||||
Gzipped |
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.
Note: You can also download the data file for the tree.
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
Seed source: | [1] |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 840 |
Number in full: | 185434 |
Average length of the domain: | 57.8 aa |
Average identity of full alignment: | 19 % |
Average coverage of the sequence by the domain: | 24.78 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 57 | ||||||||||||
Family (HMM) version: | 31 | ||||||||||||
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 CBS domain has been found. There are 1145 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.