The domain within your query sequence starts at position 45 and ends at position 204; the E-value for the GDPD domain shown below is 1.2e-26.

HRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDL
KYCELPPYLCKLDVPFQRACKCEGKDTRIPLLKEVFEAFPETPINIDIKVNNNVLIKKVS
ELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQR

GDPD

• PFAM accession number: PF03009
• Interpro abstract (IPR030395):

  This entry represents the GP-PDE domain.

  The glycerophosphodiester phosphodiesterases (GD-PDEs) were initially characterised in bacteria, where they have functional roles for production of metabolic carbon and phosphate sources from glycerophosphodiesters and in adherence to and degradation of mammalian host-cell membranes. Mammalian GP- GDEs have been identified more recently and shown to be implicated in several physiological functions. GD-PDEs are involved in glycerol metabolism and catalyze the reaction of glycerophosphodiester and water to alcohol and sn-glycerol-3-phosphate. They display broad specificity for glycerophosphodiesters, such as glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophosphoglycerol).

  The GP-PDE domain adopts the ubiquitous triosephosphate isomerase (TIM) barrel alpha/beta fold. The TIM barrel is comprised of an eight-stranded parallel beta-sheet barrel surrounded by eight alpha-helices. There is a small insertion to the conventional TIM barrel structure referred to as the GDPD-insertion (GDPD-I). The GDPD-I is comprised of beta strands, alpha-helices (H3 and H4), and 3/10 helices. Although the TIM barrel and a small insertion are unique for GP-PDE family, there are subtle differences in size and topology of each domain [ (PUBMED:15162496) (PUBMED:16909422) ].

  Some proteins known to contain a GP-PDE domain are listed below:

  • Bacterial glycerophosphoryl diester phosphodiesterase GlpQ (EC 3.1.4.46).
  • Bacterial gylcerophosphoryl diester phosphodiesterase UgpQ (EC 3.1.4.46).
  • Mammalian glycerophosphodiester phosphodiesterase 1 (GDE1) (EC 3.1.4.44) (or MMIR16) [ (PUBMED:12576545) ], an integral membrane glycoprotein that interacts with regulator of G protein signaling proteins. It hydrolyzes glycerophosphoinositols (GPIs) producing inositol and glycerol 3-phosphate.
  • Mammalian glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5) (EC 3.1.-.-) (or GDE2) [ (PUBMED:15276213) ].
  • Mammalian glycerophosphoinositol inositolphosphodiesterase GDPD2 (or GDE3) (EC 3.1.4.43) [ (PUBMED:12933806) ], up-regulated during osteoblast differentiation and can affect cell morpholgy. It hydrolyzes glycerophosphoinositol (GroPIns), producing inositol 1-phosphate and glycerol.
  • Mammalian glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1) (EC 3.1.-.-) (or GDE4) [ (PUBMED:18991142) ].
  • Mammalian glycerophosphocholine phosphodiesterase GPCPD1 (EC 3.1.4.2) (or GDE5), selectively hydrolyzes glycerophosphocholine (GroPCho) and controls skeletal muscle development [ (PUBMED:20576599) ].
  • Mammalian glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4) (EC 3.1.-.-) (or GDE6) [ (PUBMED:15276213) ].
• GO process: lipid metabolic process (GO:0006629)
• GO function: phosphoric diester hydrolase activity (GO:0008081)

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