Protein Family Models

Date:

2024-08-14

This family is often found at the very N-terminus of proteins from the phospholipase_D-nuclease family, PLDc, Pfam:PF00614. However, a large number of members are full-length within this family. (from Pfam)

Date:

2024-08-14

Phosphatidylcholine-hydrolysing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, and/or asparagine residues which may contribute to the active site. aspartic acid. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved. [1]. 8732763. A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: identification of duplicated repeats and potential active site residues. Ponting CP, Kerr ID;. Protein Sci 1996;5:914-922. [2]. 8755242. A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins. Koonin EV;. Trends Biochem Sci 1996;21:242-243. [3]. 8051126. Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D from Ricinus communis L. Wang X, Xu L, Zheng L;. J Biol Chem 1994;269:20312-20317. [4]. 9242915. Regulation of eukaryotic phosphatidylinositol-specific phosp. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This model is based on experimentally characterized bacterial cardiolipin synthases (cls) from E. coli, Staphylococcus aureus (two), and Bacillus pseudofirmus OF4. This model describes just one of several homologous but non-orthologous forms of cls. The cutoff score is set arbitrarily high to avoid false-positives. Note that there are two enzymatic activites called cardiolipin synthase. This model represents type 1, which does not rely on a CDP-linked donor, but instead does a reversible transfer of a phosphatidyl group from one phosphatidylglycerol molecule to another.

Gene:

cls

Date:

2024-05-30