Q65RN7 · DNLJ_MANSM
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids675 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 34-38 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DAEYD | ||||||
Binding site | 83-84 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 116 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 118 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 139 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 176 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 293 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 317 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 411 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 414 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 429 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 435 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | DNA binding | |
Molecular Function | DNA ligase (NAD+) activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA repair | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Basfia
Accessions
- Primary accessionQ65RN7
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000313301 | 1-675 | DNA ligase | |||
Sequence: MTIMDINQQIKQLRDTLRYHEYQYHVLDDPKIPDAEYDRLFHQLKALEQQHPELITADSPTQRVGAKPLAGFAQITHELPMLSLDNAFSDEEFNAFVKRIQDRLIVLPQPLTFCCEPKLDGLAVSIFYVNGVLTQAATRGDGTTGEDITLNIRTIRNIPLQLLTDNPPARLEVRGEVFMPHEGFNRLNERALEHGEKTFANPRNAAAGSLRQLDPKITSRRPLVFNAYSVGIAEGVELPATHYERLQWLKSVGIPVNSEVQLCDGSEKVLEFYRSMQQKRPTLGYDIDGTVLKINDIGLQRELGFISKAPRWAIAYKFPAQEELTRLNDVEFQVGRTGAITPVAKLAPVFVAGVTVSNATLHNGDEIARLDIAIGDTVVIRRAGDVIPQIIGVLHERRPANAQAIVFPTQCPVCGSKIVRIEGEAVARCTGGLFCDAQRKEALKHFVSRRAMDIDGVGAKLIEQLVDKELIRTPADLFKLDLITLMRLERMGEKSAQNALDSLEKAKNTTLARFIFALGIREVGEATALNLANHFKNLDALQAASPEQLQEVADVGEVVANRIYVFWREQHNIDAVNDLIAQGIHWETVETKEAGENPFKGKTVVLTGTLTQMGRNETKDLLQQLGAKAAGSVSAKTHFVIAGDNAGSKLTKAQELGVAVMSEAEFLAIVNAYKR |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 594-675 | BRCT | ||||
Sequence: AGENPFKGKTVVLTGTLTQMGRNETKDLLQQLGAKAAGSVSAKTHFVIAGDNAGSKLTKAQELGVAVMSEAEFLAIVNAYKR |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length675
- Mass (Da)74,740
- Last updated2004-10-25 v1
- Checksum0E204248ECD1E756
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016827 EMBL· GenBank· DDBJ | AAU38373.1 EMBL· GenBank· DDBJ | Genomic DNA |