| Analysis | rpsblast_cdd | Start | 185 |
| End | 339 | Strand | + |
| Length | 155 | Note | Gaps:11 |
| Hit Coverage | 97.04 | Hit Length | 169 |
| Hit Pident | 33.54 | E Val | 1e-25 |
| Hit Description | cd09193 PLDc_mTdp1_1 Catalytic domain repeat 1 of metazoan tyrosyl-DNA phosphodiesterase. Catalytic domain repeat 1 of metazoan tyrosyl-DNA phosphodiesterase (Tdp1 EC 3.1.4.-). Human Tdp1 (hTdp1) acts as an important DNA repair enzyme with a preference for single-stranded or blunt-ended duplex oligonucleotides. It can remove 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 therefore a potential molecular target for new anti-cancer drugs. hTdp1 has been shown to associate with additional proteins such as XRCC1 to form a multi-enzyme complex. These additional proteins may be involved in recognizing 3'-phoshotyrosyl DNA in vivo. hTdp1 is a monomeric protein containing 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. Like other PLD enzymes hTdp1 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 | 20.12 |
| Name | Qrob_P0240420.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0240420.2 | Quercus robur | 97.0 | egn | (M=2) K10862 - tyrosyl-DNA phosphodiesterase 1 [EC:3.1.4.-] | EC:3.1.4.1 | validated |
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