The domain within your query sequence starts at position 372 and ends at position 398; the E-value for the PLDc domain shown below is 6.11e0.

WARNING!
Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 10074947 ) for details.

Catalytic residues
PositionAmino acidPresent?
DomainProtein
6377HNo
13384DYes
FPKLNRNKYMVTDGAAYIGNFDWVGND

PLDc

Phospholipase D. Active site motifs.
PLDc
SMART accession number:SM00155
Description: Phosphatidylcholine-hydrolyzing 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, aspartic acid, and/or asparagine residues which may contribute to the active site. 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.
Interpro abstract (IPR001736):

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 Escherichia coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs [ (PUBMED:8732763) (PUBMED:8755242) (PUBMED:8051126) (PUBMED:9242915) ].

GO function:catalytic activity (GO:0003824)
Family alignment:
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There are 86578 PLDc domains in 45058 proteins in SMART's nrdb database.

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