lysophospholipid acyltransferase (LPLAT) family protein may act as an acyltransferase of a de novo or remodeling pathway of glycerophospholipid biosynthesis, catalyzing the incorporation of an acyl group from either acyl-CoAs or acyl-acyl carrier proteins (acyl-ACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
36-327
1.00e-114
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).
The actual alignment was detected with superfamily member pfam03982:
Pssm-ID: 473073 [Multi-domain] Cd Length: 297 Bit Score: 334.01 E-value: 1.00e-114
Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is ...
36-327
1.00e-114
Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is catalyzed by the enzyme diacylglycerol acyltransferase (DAGAT).
Pssm-ID: 112781 [Multi-domain] Cd Length: 297 Bit Score: 334.01 E-value: 1.00e-114
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
78-314
3.93e-45
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins.
Pssm-ID: 153249 [Multi-domain] Cd Length: 212 Bit Score: 152.83 E-value: 3.93e-45
Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is ...
36-327
1.00e-114
Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is catalyzed by the enzyme diacylglycerol acyltransferase (DAGAT).
Pssm-ID: 112781 [Multi-domain] Cd Length: 297 Bit Score: 334.01 E-value: 1.00e-114
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
78-314
3.93e-45
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins.
Pssm-ID: 153249 [Multi-domain] Cd Length: 212 Bit Score: 152.83 E-value: 3.93e-45
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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