The domain within your query sequence starts at position 90 and ends at position 166; the E-value for the PlsC domain shown below is 1.14e-2.
All catalytic sites are present in this domain. Check the literature (PubMed 11377195 ) for details.
AIVVLNHKFEIDFLCGWSLAERLGILGNSKVLAKKELAYVPIIGWMWYFVEMIFCTRKWE QDRQTVAKSLLHLRDYP
PlsCPhosphate acyltransferases |
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SMART accession number: | SM00563 |
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Description: | Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family. |
Interpro abstract (IPR002123): | This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function [ (PUBMED:9259571) ]. This domain is found in tafazzins, defects in which are the cause of Barth syndrome; a severe inherited disorder which is often fatal in childhood and is characterised by cardiac and skeletal abnormalities. Phospholipid/glycerol acyltransferase is not found in the viruses or the archaea and is under represented in the bacteria. Bacterial glycerol-phosphate acyltransferases are involved in membrane biogenesis since they use fatty acid chains to form the first membrane phospholipids [ (PUBMED:18369234) ]. |
GO function: | transferase activity, transferring acyl groups (GO:0016746) |
Family alignment: |
There are 106677 PlsC domains in 106607 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Disease (disease genes where sequence variants are found in this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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