Q89FV8 · DNLJ_BRADU
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids716 (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 | 50-54 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DAEYD | ||||||
Binding site | 99-100 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 132 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 134 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 155 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 192 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 308 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 332 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 437 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 439 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 461 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 467 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | DNA ligase (NAD+) activity | |
Molecular Function | metal ion binding | |
Biological Process | base-excision repair, DNA ligation | |
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 > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium
Accessions
- Primary accessionQ89FV8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000313149 | 1-716 | DNA ligase | |||
Sequence: MMARAAKSKPLRDVAELTKAQAKVELMRLALELEGHDKRYYQDDAPTVTDAEYDALRQRFNAIEKRFPEFVSAESPSQKVGAAPSGRFRKVRHAVPMLSLDNAFAEEDVRDFVGRIVRFLKLDDDKIDFSAEPKIDGLSMSLRYEGGELVTAATRGDGAEGEDVTANIRTLEDVPQKLKGRNVPDICEVRGEVYMTKKAFLALNERQKAAGDTIFANPRNSAAGSLRQKDPTITASRPLGFFAYAWGEMSAMPEETQTGMIHWFERCGFKTNPLTRLCHSVEELIAFHQRIEEERAELDYDIDGVVYKVDRIDWQERLGFVSRTPRWGIAHKFPAEQAMTVLRDIEIQVGRTGSFTPVGKLEPVGVGGVIVQNVTLHNEDYIKGIGNKGEVLREGRDIRIGDTVVIQRAGDVIPQVVDVVLDKRPKTAKEFHFPKTCPCPLHTDVTREETAAGEEGSRARCTGEFACPYQKIEHLKLFVSRRAFDIDGLGEKQLQYFFDEGFVKEPADIFTLEKRNAKLKLEEIEGYGATSVRNLFAAIESRRRIALERFVYALGMRHVGETTALALARGYGSWEAFHDACLKVAKGDEEAMADMDALDQIGDTVIKSIADYFGESHNRGIVERLTKEVEIVDAEKPKSNSAVAGKTVVFTGSLEKMTRDEAKATAERLGAKVSGSVSKKTDLVVAGPGAGSKLAEANKHGVKVLTEDEWLKLIGE |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 638-716 | BRCT | ||||
Sequence: KSNSAVAGKTVVFTGSLEKMTRDEAKATAERLGAKVSGSVSKKTDLVVAGPGAGSKLAEANKHGVKVLTEDEWLKLIGE |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length716
- Mass (Da)79,565
- Last updated2003-06-01 v1
- ChecksumE31CDDC5B2928161
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000040 EMBL· GenBank· DDBJ | BAC51856.1 EMBL· GenBank· DDBJ | Genomic DNA |