phosphatidate phosphatase is a magnesium-dependent enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
714-939
2.10e-144
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.
:
Pssm-ID: 462403 Cd Length: 226 Bit Score: 430.39 E-value: 2.10e-144
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
1-104
1.04e-55
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.
:
Pssm-ID: 461356 Cd Length: 103 Bit Score: 187.75 E-value: 1.04e-55
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
516-628
1.89e-41
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.
:
Pssm-ID: 465292 Cd Length: 98 Bit Score: 147.05 E-value: 1.89e-41
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
714-939
2.10e-144
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.
Pssm-ID: 462403 Cd Length: 226 Bit Score: 430.39 E-value: 2.10e-144
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
762-917
1.09e-89
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.
Pssm-ID: 197870 Cd Length: 157 Bit Score: 283.78 E-value: 1.09e-89
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
1-104
1.04e-55
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.
Pssm-ID: 461356 Cd Length: 103 Bit Score: 187.75 E-value: 1.04e-55
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
516-628
1.89e-41
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.
Pssm-ID: 465292 Cd Length: 98 Bit Score: 147.05 E-value: 1.89e-41
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
714-939
2.10e-144
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.
Pssm-ID: 462403 Cd Length: 226 Bit Score: 430.39 E-value: 2.10e-144
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
762-917
1.09e-89
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.
Pssm-ID: 197870 Cd Length: 157 Bit Score: 283.78 E-value: 1.09e-89
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
1-104
1.04e-55
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.
Pssm-ID: 461356 Cd Length: 103 Bit Score: 187.75 E-value: 1.04e-55
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
516-628
1.89e-41
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.
Pssm-ID: 465292 Cd Length: 98 Bit Score: 147.05 E-value: 1.89e-41
Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region ...
763-878
3.53e-04
Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region found in Phosphatidate phosphatase APP1 from yeast, which contains the catalytic motif DXDX(T/V), present in other Mg+2-dependent phosphatases. This domain has a weak sequence similarity to the haloacid dehalogenase-like domain. APP1 catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol and may play a role in vesicular trafficking through its phosphatidate phosphatase activity at cortical actin patches.
Pssm-ID: 462930 Cd Length: 153 Bit Score: 42.10 E-value: 3.53e-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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if a domain or superfamily has been annotated with functional sites (conserved features),
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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