| Analysis | rpsblast_cdd | Start | 54 |
| End | 167 | Strand | + |
| Length | 114 | Note | Gaps:23 |
| Hit Coverage | 43.00 | Hit Length | 300 |
| Hit Pident | 26.36 | E Val | 2e-14 |
| Hit Description | cd08621 PI-PLCXDc_like_2 Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi which are similar to eukaryotic phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain X domain and are more closely related to bacterial PI-PLCs which participate in Ca2+-independent PI metabolism hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear it may distinct from that of typical eukaryotic PI-PLCs. | Hit Pcons | 13.18 |
| Name | Qrob_P0274880.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0274880.2 | Quercus robur | 100.0 | egn | (M=1) 4.6.1.13 - Phosphatidylinositol diacylglycerol-lyase. | EC:3.1.4.11, EC:4.6.1.13 | validated |
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