| Analysis | rpsblast_cdd | Start | 43 |
| End | 306 | Strand | + |
| Length | 264 | Note | Gaps:25 |
| Hit Coverage | 100.00 | Hit Length | 277 |
| Hit Pident | 37.91 | E Val | 6e-74 |
| Hit Description | cd07378 MPP_ACP5 Homo sapiens acid phosphatase 5 and related proteins metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse but all share a conserved domain with an active site consisting of two metal ions (usually manganese iron or zinc) coordinated with octahedral geometry by a cage of histidine aspartate and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases Dbr1-like RNA lariat debranching enzymes YfcE-like phosphodiesterases purple acid phosphatases (PAPs) YbbF-like UDP-2 3-diacylglucosamine hydrolases and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. | Hit Pcons | 9.75 |
| Name | Qrob_P0117900.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0117900.2 | Quercus robur | 100.0 | egn | (M=2) 1.11.1.7//3.1.3.2 - Peroxidase. // Acid phosphatase. | EC:3.1.3.2, EC:1.11.1.7 | validated |
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