diacylglycerol kinase catalytic domain-containing protein is involved in the conversion of diacylglycerol (DAG) to phosphatidic acid (PA), utilizing ATP as a source of the phosphate
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
188-611
6.20e-51
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. 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.
The actual alignment was detected with superfamily member PLN02204:
Pssm-ID: 445337 [Multi-domain] Cd Length: 601 Bit Score: 185.86 E-value: 6.20e-51
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
204-347
7.15e-27
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. 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.
Pssm-ID: 425868 [Multi-domain] Cd Length: 125 Bit Score: 105.75 E-value: 7.15e-27
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
206-338
2.46e-11
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.
Pssm-ID: 214487 [Multi-domain] Cd Length: 124 Bit Score: 61.16 E-value: 2.46e-11
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
203-347
6.83e-04
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 161732 [Multi-domain] Cd Length: 293 Bit Score: 42.11 E-value: 6.83e-04
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
204-347
7.15e-27
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. 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.
Pssm-ID: 425868 [Multi-domain] Cd Length: 125 Bit Score: 105.75 E-value: 7.15e-27
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
206-338
2.46e-11
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.
Pssm-ID: 214487 [Multi-domain] Cd Length: 124 Bit Score: 61.16 E-value: 2.46e-11
Ceramide kinase C-terminal domain; This domain is found at the C-terminus of ceramide kinase ...
393-600
4.65e-06
Ceramide kinase C-terminal domain; This domain is found at the C-terminus of ceramide kinase enzymes. It is related to the beta sandwich domain of NAD kinases. Along with the N-terminal domain it catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. This family contains ceramide kinase like proteins that lack the ceramide kinase activity. It also contains ore distantly related proteins this may have different functions.
Pssm-ID: 466025 Cd Length: 222 Bit Score: 48.16 E-value: 4.65e-06
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
203-347
6.83e-04
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 161732 [Multi-domain] Cd Length: 293 Bit Score: 42.11 E-value: 6.83e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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