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3  structures 3038  species 0  interactions 3222  sequences 7  architectures

Family: DAGK_prokar (PF01219)

Summary: Prokaryotic diacylglycerol kinase

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

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Diacylglycerol kinase Edit Wikipedia article

Prokaryotic diacylglycerol kinase
Soluble diacylglycerol kinase DgkB from Staphylococcus aureus.png
DgkB, soluble DAGK from Staphylococcus aureus. α-helices in red, β-strands in yellow, coils in green.
Identifiers
Symbol DAGK_prokar
Pfam PF01219
InterPro IPR000829
PROSITE PDOC00820
OPM superfamily 217
OPM protein 2kdc
Diacylglycerol kinase catalytic domain
Identifiers
Symbol DAGK_cat
Pfam PF00781
Pfam clan CL0240
InterPro IPR001206
SMART DAGKc
Diacylglycerol kinase accessory domain
Identifiers
Symbol DAGK_acc
Pfam PF00609
InterPro IPR000756
SMART DAGKa

Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another.[1]

In bacteria, DGK is very small (13 to 15 kD) membrane protein which seems to contain three transmembrane domains.[2] The best conserved region is a stretch of 12 residues which are located in a cytoplasmic loop between the second and third transmembrane domains. Some Gram-positive bacteria also encode a soluble diacylglycerol kinase capable of reintroducing DAG into the phospholipid biosynthesis pathway. DAG accumulates in Gram-positive bacteria as a result of the transfer of glycerol-1-phosphate moieties from phosphatidylglycerol to lipotechoic acid.[3]

Mammalian DGK Isoforms[edit]

Currently, nine members of the DGK family have been cloned and identified. Although all family members have conserved catalytic domains and two cysteine rich domains, they are further classified into five groups according to the presence of additional functional domains and substrate specificity.[4] These are as follows:

  • Type 1 - DGK-α, DGK-β, DGK-γ - contain EF-hand motifs and a recoverin homology domain
  • Type 2 - DGK-δ, DGK-η - contain a pleckstrin homology domain
  • Type 3 - DGK-ε - has specificity for arachidonate-containing DAG
  • Type 4 - DGK-ζ, DGK-ι - contain a MARCKS homology domain, ankyrin repeats, a C-terminal nuclear localisation signal, and a PDZ-binding motif.
  • Type 5 - DGK-θ - contains a third cysteine-rich domain, a pleckstrin homology domain and a proline rich region

References[edit]

  1. ^ Merida I, Avila-Flores A, Merino E (2008). "Diacylglycerol kinases: at the hub of cell signalling.". Biochem. J. 409 (1): 1–18. doi:10.1042/BJ20071040. PMID 18062770. 
  2. ^ Smith RL, O'Toole JF, Maguire ME, Sanders CR (September 1994). "Membrane topology of Escherichia coli diacylglycerol kinase". J. Bacteriol. 176 (17): 5459–65. PMC 196734. PMID 8071224. 
  3. ^ Miller DJ, Jerga A, Rock CO, White SW (July 2008). "Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluable diacylglycol kinases". Structure 16 (7): 1036–46. doi:10.1016/j.str.2008.03.019. PMID 18611377. 
  4. ^ Van Blitterswijk, WJ, and Houssa, B (2000). "Properties and functions of diacylglycerol kinases.". Cellular Signaling 1 (9-10): 595–605. PMID 11080611. 

External links[edit]

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000829

Diacylglycerol kinase (EC) (DAGK) is an enzyme that catalyses the formation of phosphatidic acid from diacylglycerol and ATP, an important step in phospholipid biosynthesis. In bacteria DAGK is very small (13 to 15 kD) membrane protein which seems to contain three transmembrane domains [PUBMED:8071224]. The best conserved region, is a stretch of 12 residues which are located in a cytoplasmic loop between the second and third transmembrane domains.

Gene Ontology

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Domain organisation

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Alignments

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  Seed
(186)
Full
(3222)
Representative proteomes NCBI
(1802)
Meta
(403)
RP15
(181)
RP35
(367)
RP55
(508)
RP75
(605)
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  Seed
(186)
Full
(3222)
Representative proteomes NCBI
(1802)
Meta
(403)
RP15
(181)
RP35
(367)
RP55
(508)
RP75
(605)
Alignment:
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  Seed
(186)
Full
(3222)
Representative proteomes NCBI
(1802)
Meta
(403)
RP15
(181)
RP35
(367)
RP55
(508)
RP75
(605)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
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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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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.

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Curation and family details

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Seed source: Prosite
Previous IDs: none
Type: Family
Author: Finn RD, Bateman A
Number in seed: 186
Number in full: 3222
Average length of the domain: 102.60 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 78.24 %

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 21.9 21.9
Trusted cut-off 22.4 25.2
Noise cut-off 21.5 21.6
Model length: 104
Family (HMM) version: 14
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 DAGK_prokar domain has been found. There are 3 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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