Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
1145  structures 8987  species 0  interactions 185434  sequences 1197  architectures

Family: CBS (PF00571)

Summary: CBS domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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

  1. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)
  2. ^ 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. {{cite journal}}: Unknown parameter |month= ignored (help)
  3. ^ 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. {{cite journal}}: Explicit use of et al. in: |author= (help); Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

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

  1. 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

  2. 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

  3. 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

  4. 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

  5. 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

  6. 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

External database links

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...

Loading domain graphics...

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...

View options

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)
Representative proteomes UniProt
(735709)
RP15
(25040)
RP35
(85562)
RP55
(181009)
RP75
(301618)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(840)
Full
(185434)
Representative proteomes UniProt
(735709)
RP15
(25040)
RP35
(85562)
RP55
(181009)
RP75
(301618)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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
(840)
Full
(185434)
Representative proteomes UniProt
(735709)
RP15
(25040)
RP35
(85562)
RP55
(181009)
RP75
(301618)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped 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.

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 View help on the curation process

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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.0 16.5
Trusted cut-off 24.0 16.5
Noise cut-off 23.9 16.4
Model length: 57
Family (HMM) version: 31
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

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

Selections

Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

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

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

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.

Loading structure mapping...

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.

Protein Predicted structure External Information
A0A044QL93 View 3D Structure Click here
A0A044QT05 View 3D Structure Click here
A0A044SG85 View 3D Structure Click here
A0A044SZZ3 View 3D Structure Click here
A0A044T0R2 View 3D Structure Click here
A0A044T2T7 View 3D Structure Click here
A0A044V4F4 View 3D Structure Click here
A0A044VFN8 View 3D Structure Click here
A0A077Z319 View 3D Structure Click here
A0A077Z3E9 View 3D Structure Click here
A0A077ZA63 View 3D Structure Click here
A0A077ZF52 View 3D Structure Click here
A0A077ZGW2 View 3D Structure Click here
A0A077ZJ53 View 3D Structure Click here
A0A077ZJA9 View 3D Structure Click here
A0A077ZK54 View 3D Structure Click here
A0A077ZL24 View 3D Structure Click here
A0A0D2DYQ8 View 3D Structure Click here
A0A0D2E830 View 3D Structure Click here
A0A0D2E8A1 View 3D Structure Click here
A0A0D2G315 View 3D Structure Click here
A0A0D2G7P5 View 3D Structure Click here
A0A0D2H1A0 View 3D Structure Click here
A0A0G2KKC2 View 3D Structure Click here
A0A0H3GQ71 View 3D Structure Click here
A0A0H3GQQ5 View 3D Structure Click here
A0A0H3GSK7 View 3D Structure Click here
A0A0H3GVE4 View 3D Structure Click here
A0A0H3GW25 View 3D Structure Click here
A0A0H3GWM8 View 3D Structure Click here
A0A0H3GX14 View 3D Structure Click here
A0A0H3H0X8 View 3D Structure Click here
A0A0H3H1U0 View 3D Structure Click here
A0A0H3H331 View 3D Structure Click here
A0A0H3H3K6 View 3D Structure Click here
A0A0H5S1A5 View 3D Structure Click here
A0A0H5S3I7 View 3D Structure Click here
A0A0H5S9G5 View 3D Structure Click here
A0A0J9Y2D3 View 3D Structure Click here
A0A0K0DSJ3 View 3D Structure Click here