| Analysis | rpsblast_cdd | Start | 48 |
| End | 334 | Strand | + |
| Length | 287 | Note | Gaps:26 |
| Hit Coverage | 98.25 | Hit Length | 286 |
| Hit Pident | 35.59 | E Val | 6e-47 |
| Hit Description | cd08606 GDPD_YPL110cp_fungi Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1) YPL110cp (Gde1p) displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE EC 3.1.4.46) which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC not glycerophosphoinositol (GPI) to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture including not only C-terminal GDPD but also an SPX N-terminal domain along with several ankyrin repeats which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp which selectively catalyzes the cleavage of phosphatidylglycerol (PG) not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC) to diacylglycerol (DAG) and glycerophosphate and has been characterized as a PG-specific phospholipase C. | Hit Pcons | 17.44 |
| Name | Qrob_P0187470.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0187470.2 | Quercus robur | 100.0 | egn | (M=2) PTHR22958 - RELATED TO MULTIFUNCTIONAL CYCLIN-DEPENDENT KINASE-RELATED | EC:3.1.4.46 | validated |
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