| Analysis | rpsblast_cdd | Start | 22 |
| End | 50 | Strand | + |
| Length | 29 | Note | none |
| Hit Coverage | 12.89 | Hit Length | 225 |
| Hit Pident | 62.07 | E Val | 1e-09 |
| Hit Description | cd07903 Adenylation_DNA_ligase_IV Adenylation domain of DNA Ligase IV. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication recombination and repair. ATP-dependent ligases are present in many organisms such as viruses bacteriophages eukarya archaea and bacteria. There are three classes of ATP-dependent DNA ligase in eukaryotic cells (I III and IV). DNA ligase IV is required for DNA non-homologous end joining pathways including recombination of the V(D)J immunoglobulin gene segments in cells of the mammalian immune system. DNA ligase IV is stabilized by forming a complex with XRCC4 a nuclear phosphoprotein which is phosphorylated by DNA-dependent protein kinase. DNA ligases have a highly modular architecture consisting of a unique arrangement of two or more discrete domains. The adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains comprise a catalytic core unit that is common to all members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. The common catalytic unit comprises six conserved sequence motifs (I III IIIa IV V and VI) that define this family of related nucleotidyltransferases. | Hit Pcons | 20.69 |
| Name | Qrob_P0078600.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0078600.2 | Quercus robur | 99.1 | egn | (M=2) 6.5.1.1 - DNA ligase (ATP). | EC:6.5.1.1 | validated |
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