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0  structures 829  species 0  interactions 10032  sequences 232  architectures

Family: DAGK_acc (PF00609)

Summary: Diacylglycerol kinase accessory 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 "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 accessory domain Provide feedback

Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.

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


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000756

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [ PUBMED:3291115 ]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function is evolutionarily conserved from Escherichia coli to human [ PUBMED:12471243 ]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [ PUBMED:12368087 ]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [ PUBMED:15078142 ], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [ PUBMED:15320712 ].

Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The DAG kinase domain is assumed to be an accessory domain. Upon cell stimulation, DAG kinase converts DAG into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It catalyses the reaction: ATP + 1,2-diacylglycerol = ADP + 1,2-diacylglycerol 3-phosphate. The enzyme is stimulated by calcium and phosphatidylserine and phosphorylated by protein kinase C. This domain is always associated with 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 NAD_kinase_C (CL0701), which has the following description:

This superfamily includes families that are related to the C-terminal beta sandwich domain of NAD kinase. It includes the YegS C-terminal domain, the accessory domains from Diacylglycerol kinase and the ceramide kinase C-terminal domain.

The clan contains the following 4 members:

CERK_C DAGK_acc NAD_kinase_C YegS_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 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
(32)
Full
(10032)
Representative proteomes UniProt
(15510)
RP15
(1315)
RP35
(3177)
RP55
(7449)
RP75
(10290)
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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
(32)
Full
(10032)
Representative proteomes UniProt
(15510)
RP15
(1315)
RP35
(3177)
RP55
(7449)
RP75
(10290)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(32)
Full
(10032)
Representative proteomes UniProt
(15510)
RP15
(1315)
RP35
(3177)
RP55
(7449)
RP75
(10290)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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: SMART
Previous IDs: DAGKa;
Type: Family
Sequence Ontology: SO:0100021
Author: Ponting CP , Schultz J, Bork P
Number in seed: 32
Number in full: 10032
Average length of the domain: 154.1 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 19.09 %

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 27.0 27.0
Trusted cut-off 27.0 27.1
Noise cut-off 26.9 26.9
Model length: 160
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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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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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
A0A044SL15 View 3D Structure Click here
A0A044TAC5 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
A0A096S3Z9 View 3D Structure Click here
A0A096UWG9 View 3D Structure Click here
A0A0K0E0W1 View 3D Structure Click here
A0A0K0EBU9 View 3D Structure Click here
A0A0K0EED4 View 3D Structure Click here
A0A0K0EMC4 View 3D Structure Click here
A0A0K0J4G3 View 3D Structure Click here
A0A0N4U527 View 3D Structure Click here
A0A0N4UND0 View 3D Structure Click here
A0A0R0GW00 View 3D Structure Click here
A0A0R0H4I6 View 3D Structure Click here
A0A0R0HEZ8 View 3D Structure Click here
A0A140LH08 View 3D Structure Click here
A0A158Q5V5 View 3D Structure Click here
A0A1D5NSE1 View 3D Structure Click here
A0A1D6IXW6 View 3D Structure Click here
A0A1D6K5X0 View 3D Structure Click here
A0A1D6N9T9 View 3D Structure Click here
A0A2R8Q067 View 3D Structure Click here
A0A2R8Q6P7 View 3D Structure Click here
A0A2R8Q6S0 View 3D Structure Click here
A0A2R8QAR8 View 3D Structure Click here
A0A2R8QC93 View 3D Structure Click here
A0A2R8RZP8 View 3D Structure Click here
A0A368UI28 View 3D Structure Click here
A0A3P7DVM7 View 3D Structure Click here
A0A3P7E9V6 View 3D Structure Click here
A0A3Q0KEG1 View 3D Structure Click here
A0A3Q0KRN9 View 3D Structure Click here
A0A5K4ECE7 View 3D Structure Click here
A0A5K4FES7 View 3D Structure Click here
A0JN54 View 3D Structure Click here
A4HX26 View 3D Structure Click here