SMART: Pfam domain Zn_dep

The domain within your query sequence starts at position 28 and ends at position 219; the E-value for the Zn_dep_PLPC domain shown below is 9.8e-28.

THVEIGHRALEFLRLQDGRINYKELILEHQDAYQAGTVFPDAFYPSICKRGKYHDVSERT
HWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGITSHMVADVSWHSLGIEQGFLRTMGA
IDFYNSYSDAHSAGDFGGDVLSQFEFNFNYLSRRWYVPVRDLLRIYDNLYGRKVITKDVL
VDCTYLQFLEMH

Zn_dep_PLPC

PFAM accession number:	PF00882
Interpro abstract (IPR029002):	This domain is found in bacterial zinc-dependent phospholipase C and in eukaryotic phosphatidylinositol-glycan-specific phospholipase D. Bacterial phospholipase C is a zinc-dependent enzyme, binding 3 zinc ions per molecule [ (PUBMED:2111259) ]. This enzyme catalyses the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate. Phosphatidylinositol-glycan-specific phospholipase D is an extracellular amphiphilic glycoprotein [ (PUBMED:1606959) (PUBMED:2017684) ]. It hydrolyses the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, releasing these proteins from the membrane.

PFAM accession number:

PF00882

Interpro abstract (IPR029002):

This domain is found in bacterial zinc-dependent phospholipase C and in eukaryotic phosphatidylinositol-glycan-specific phospholipase D.

Bacterial phospholipase C is a zinc-dependent enzyme, binding 3 zinc ions per molecule [ (PUBMED:2111259) ]. This enzyme catalyses the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate. Phosphatidylinositol-glycan-specific phospholipase D is an extracellular amphiphilic glycoprotein [ (PUBMED:1606959) (PUBMED:2017684) ]. It hydrolyses the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, releasing these proteins from the membrane.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Zn_dep_PLPC