Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003909 | molecular_function | DNA ligase activity |
A | 0003910 | molecular_function | DNA ligase (ATP) activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006260 | biological_process | DNA replication |
A | 0006281 | biological_process | DNA repair |
A | 0006310 | biological_process | DNA recombination |
A | 0006974 | biological_process | DNA damage response |
A | 0016874 | molecular_function | ligase activity |
A | 0044423 | cellular_component | virion component |
A | 0046872 | molecular_function | metal ion binding |
A | 0051301 | biological_process | cell division |
Functional Information from PROSITE/UniProt
site_id | PS00333 |
Number of Residues | 28 |
Details | DNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGAIVRnangp...YEpgynnyHsahlaKLK |
Chain | Residue | Details |
A | GLU291-LYS318 | |
site_id | PS00697 |
Number of Residues | 9 |
Details | DNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. QRKRNGVRA |
Chain | Residue | Details |
A | GLN149-ALA157 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI2 |
Number of Residues | 196 |
Details | Region: {"description":"AD domain","evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"N6-AMP-lysine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10135","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Site: {"description":"Important for the catalytic efficiency","evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]} |