| Analysis | rpsblast_cdd | Start | 111 |
| End | 249 | Strand | + |
| Length | 139 | Note | Gaps:12 |
| Hit Coverage | 100.00 | Hit Length | 145 |
| Hit Pident | 42.76 | E Val | 9e-41 |
| Hit Description | cd09122 PLDc_Tdp1_1 Catalytic domain repeat 1 of Tyrosyl-DNA phosphodiesterase. Catalytic domain repeat 1 of Tyrosyl-DNA phosphodiesterase (Tdp1 EC 3.1.4.-) which exists in eukaryotes but not in prokaryotes. Tdp1 acts as an important DNA repair enzyme that removes stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of a phosphodiester bond between a tyrosine side chain and a DNA 3'-phosphate. It is a monomeric protein that contains two copies of a variant HKD motif (H-x-K-x(4)-D where x represents any amino acid residue) which consists of the highly conserved histidine and lysine residues but lacks the aspartate residue that is well conserved in other phospholipase D (PLD EC 3.1.4.4) enzymes. Thus this family represents a distinct class within the PLD superfamily. Like other PLD enzymes Tdp1 may utilize a common two-step general acid/base catalytic mechanism involving a DNA-enzyme intermediate to cleave phosphodiester bonds. A single active site involved in phosphatidyl group transfer would be formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. | Hit Pcons | 15.86 |
| Name | Qrob_P0240460.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0240460.2 | Quercus robur | 0.0 | egn | (M=2) K10862 - tyrosyl-DNA phosphodiesterase 1 [EC:3.1.4.-] | EC:3.1.4.1 | validated |
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