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51  structures 6835  species 0  interactions 27760  sequences 393  architectures

Family: DAGK_cat (PF00781)

Summary: Diacylglycerol kinase catalytic domain

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This is the Wikipedia entry entitled "Diacylglycerol kinase". More...

Diacylglycerol kinase Edit Wikipedia article

Diacylglycerol Kinase (DGK) is an integral membrane protein that is expressed in E. coli. DGK has 121-residues and is a trimeric enzyme. DGK catalyzes the conversion of diacylglycerol (with ATP) to phosphatidic acid.

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.

Diacylglycerol kinase catalytic domain Provide feedback

Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologues. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family [5].

Literature references

  1. Sakane F, Yamada K, Kanoh H, Yokoyama C, Tanabe T; , Nature 1990;344:345-348.: Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. PUBMED:2156169 EPMC:2156169

  2. Sakane F, Imai S, Kai M, Wada I, Kanoh H; , J Biol Chem 1996;271:8394-8401.: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. PUBMED:8626538 EPMC:8626538

  3. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL; , FEBS Lett 1990;275:151-158.: Purification, cDNA-cloning and expression of human diacylglycerol kinase. PUBMED:2175712 EPMC:2175712

  4. Kanoh H, Yamada K, Sakane F; , Trends Biochem Sci 1990;15:47-50.: Diacylglycerol kinase: a key modulator of signal transduction? PUBMED:2159661 EPMC:2159661

  5. Bakali HM, Herman MD, Johnson KA, Kelly AA, Wieslander A, Hallberg BM, Nordlund P; , J Biol Chem. 2007;282:19644-19652.: Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. PUBMED:17351295 EPMC:17351295

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001206

The DAG-kinase catalytic domain or DAGKc domain is present in mammalian lipid kinases, such as diacylglycerol (DAG), ceramide and sphingosine kinases, as well as in related bacterial proteins [ PUBMED:8626538 , PUBMED:17351295 ]. Eukaryotic DAG-kinase ( EC ) catalyses the phosphorylation of DAG to phosphatidic acid, thus modulating the balance between the two signaling lipids. At least ten different isoforms have been identified in mammals, which form 5 groups characterised by different functional domains, such as the calcium-binding EF hand (see PROSITEDOC ), PH (see PROSITEDOC ), SAM (see PROSITEDOC ) , DAG/PE-binding C1 domain (see PROSITEDOC ) and ankyrin repeats (see PROSITEDOC ) [ PUBMED:17512245 ].

In bacteria, an integral membrane DAG kinase forms a homotrimeric protein that lacks the DAGKc domain (see PROSITEDOC ). In contrast, the bacterial yegS protein is a soluble cytosolic protein that contains the DAGKc domain in the N-terminal part. YegS is a lipid kinase with two structural domains, wherein the active site is located in the interdomain cleft, C-terminal to the DAGKc domain which forms an alpha/beta fold [ PUBMED:17351295 ]. The tertiary structure resembles that of NAD kinases and contains a metal-binding site in the C-terminal region [ PUBMED:17351295 , PUBMED:19112175 ].

This domain is usually associated with an accessory domain (see INTERPRO ).

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 PFK (CL0240), which has the following description:

This clan includes two SCOP superfamilies. Strong similarities between NAD kinases, DAG kinase, sphingosine kinase and PFK have previously been shown[1].

The clan contains the following 4 members:

DAGK_cat NAD_kinase PFK Pfk_N


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.

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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.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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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...


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: Alignment kindly provided by SMART
Previous IDs: DAGKc;
Type: Family
Sequence Ontology: SO:0100021
Author: SMART, Coggill P
Number in seed: 105
Number in full: 27760
Average length of the domain: 124 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 22.72 %

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 23.6 20.8
Trusted cut-off 23.6 20.8
Noise cut-off 23.5 20.7
Model length: 127
Family (HMM) version: 27
Download: download the raw HMM for this family

Species distribution

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Colour assignments

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


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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...

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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 DAGK_cat domain has been found. There are 51 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.

Protein Predicted structure External Information
A0A044QK65 View 3D Structure Click here
A0A044R296 View 3D Structure Click here
A0A044RMA4 View 3D Structure Click here
A0A044SL15 View 3D Structure Click here
A0A044TAC5 View 3D Structure Click here
A0A044TFZ5 View 3D Structure Click here
A0A077YZT9 View 3D Structure Click here
A0A077Z1I6 View 3D Structure Click here
A0A077Z2Z5 View 3D Structure Click here
A0A077ZB33 View 3D Structure Click here
A0A077ZBW2 View 3D Structure Click here
A0A077ZGQ6 View 3D Structure Click here
A0A096S3Z9 View 3D Structure Click here
A0A096UWG9 View 3D Structure Click here
A0A0D2F7Z1 View 3D Structure Click here
A0A0D2H2Y4 View 3D Structure Click here
A0A0G2KKM6 View 3D Structure Click here
A0A0H3GVW9 View 3D Structure Click here
A0A0K0E0W1 View 3D Structure Click here
A0A0K0EBU9 View 3D Structure Click here
A0A0K0ECP7 View 3D Structure Click here
A0A0K0EED4 View 3D Structure Click here
A0A0K0EH37 View 3D Structure Click here
A0A0K0EIH1 View 3D Structure Click here
A0A0K0EKT8 View 3D Structure Click here
A0A0K0EMC4 View 3D Structure Click here
A0A0K0J4G3 View 3D Structure Click here
A0A0N4U105 View 3D Structure Click here
A0A0N4U527 View 3D Structure Click here
A0A0N4UI97 View 3D Structure Click here
A0A0N4UJK6 View 3D Structure Click here
A0A0N4UND0 View 3D Structure Click here
A0A0P0V8X5 View 3D Structure Click here
A0A0R0GTJ7 View 3D Structure Click here
A0A0R0HEZ8 View 3D Structure Click here
A0A0R0JBW8 View 3D Structure Click here
A0A0R4IC42 View 3D Structure Click here
A0A140LH08 View 3D Structure Click here
A0A158Q5V5 View 3D Structure Click here
A0A175VVK5 View 3D Structure Click here