CDP-alcohol phosphatidyltransferase family protein similar to phosphatidylcholine/phosphatidylserine synthase, which catalyzes the condensation of CDP-diacylglycerol with choline or L-serine to form phosphatidylcholine or (3-sn-phosphatidyl)-L-serine, respectively
CDP-diacylglycerol--serine O-phosphatidyltransferase; This enzyme, CDP-diacylglycerol--serine ...
27-184
2.85e-26
CDP-diacylglycerol--serine O-phosphatidyltransferase; This enzyme, CDP-diacylglycerol--serine O-phosphatidyltransferase, is involved in phospholipid biosynthesis catalyzing the reaction CDP-diacylglycerol + L-serine = CMP + L-1-phosphatidylserine. Members of this family do not bear any significant sequence similarity to the corresponding E.coli protein. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273098 Cd Length: 151 Bit Score: 100.98 E-value: 2.85e-26
CDP-alcohol phosphatidyltransferase; All of these members have the ability to catalyze the ...
15-123
3.86e-18
CDP-alcohol phosphatidyltransferase; All of these members have the ability to catalyze the displacement of CMP from a CDP-alcohol by a second alcohol with formation of a phosphodiester bond and concomitant breaking of a phosphoride anhydride bond.
Pssm-ID: 460049 [Multi-domain] Cd Length: 157 Bit Score: 79.52 E-value: 3.86e-18
protein sorting system archaetidylserine synthase; Members of this family are homologs of ...
29-184
1.47e-07
protein sorting system archaetidylserine synthase; Members of this family are homologs of CDP-diacylglycerol--serine O-phosphatidyltransferase PssA of subclass II, as found in Gram-positive bacteria, but occur in a branch of the archaea. In Haloferax volcanii, the member of this family HVO_1143, together with the PssD-related decarboxylase HVO_0146, were both shown to be required for the archaeosortase ArtA to cause removal of the PGF-CTERM sorting signal and replacement with a prenyl-derived C-terminal lipid anchor. Based on these observations, members of this family are suggested to be CDP-2,3-di-O-geranylgeranyl-sn-glycerol:l-serine O-archaetidyltransferase, generating archaetidylserine en route to archaetidylethanolamine biosynthesis.
Pssm-ID: 468342 [Multi-domain] Cd Length: 222 Bit Score: 51.18 E-value: 1.47e-07
CDP-diacylglycerol--serine O-phosphatidyltransferase; This enzyme, CDP-diacylglycerol--serine ...
27-184
2.85e-26
CDP-diacylglycerol--serine O-phosphatidyltransferase; This enzyme, CDP-diacylglycerol--serine O-phosphatidyltransferase, is involved in phospholipid biosynthesis catalyzing the reaction CDP-diacylglycerol + L-serine = CMP + L-1-phosphatidylserine. Members of this family do not bear any significant sequence similarity to the corresponding E.coli protein. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273098 Cd Length: 151 Bit Score: 100.98 E-value: 2.85e-26
CDP-alcohol phosphatidyltransferase; All of these members have the ability to catalyze the ...
15-123
3.86e-18
CDP-alcohol phosphatidyltransferase; All of these members have the ability to catalyze the displacement of CMP from a CDP-alcohol by a second alcohol with formation of a phosphodiester bond and concomitant breaking of a phosphoride anhydride bond.
Pssm-ID: 460049 [Multi-domain] Cd Length: 157 Bit Score: 79.52 E-value: 3.86e-18
Phosphatidylglycerophosphate synthase [Lipid transport and metabolism]; ...
17-117
9.57e-13
Phosphatidylglycerophosphate synthase [Lipid transport and metabolism]; Phosphatidylglycerophosphate synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 440324 [Multi-domain] Cd Length: 177 Bit Score: 65.27 E-value: 9.57e-13
protein sorting system archaetidylserine synthase; Members of this family are homologs of ...
29-184
1.47e-07
protein sorting system archaetidylserine synthase; Members of this family are homologs of CDP-diacylglycerol--serine O-phosphatidyltransferase PssA of subclass II, as found in Gram-positive bacteria, but occur in a branch of the archaea. In Haloferax volcanii, the member of this family HVO_1143, together with the PssD-related decarboxylase HVO_0146, were both shown to be required for the archaeosortase ArtA to cause removal of the PGF-CTERM sorting signal and replacement with a prenyl-derived C-terminal lipid anchor. Based on these observations, members of this family are suggested to be CDP-2,3-di-O-geranylgeranyl-sn-glycerol:l-serine O-archaetidyltransferase, generating archaetidylserine en route to archaetidylethanolamine biosynthesis.
Pssm-ID: 468342 [Multi-domain] Cd Length: 222 Bit Score: 51.18 E-value: 1.47e-07
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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