| Analysis | rpsblast_cdd | Start | 3 |
| End | 259 | Strand | + |
| Length | 257 | Note | Gaps:5 |
| Hit Coverage | 100.00 | Hit Length | 262 |
| Hit Pident | 64.12 | E Val | 1e-135 |
| Hit Description | cd00844 MPP_Dbr1_N Dbr1 RNA lariat debranching enzyme N-terminal metallophosphatase domain. Dbr1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' phosphodiester bonds at the branch points of excised intron lariats. This alignment model represents the N-terminal metallophosphatase domain of Dbr1. This domain 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 | 12.98 |
| Name | Qrob_P0272020.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0272020.2 | Quercus robur | 11.0 | egn | (M=1) K18328 - lariat debranching enzyme [EC:3.1.-.-] | validated |
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