D0KWN0 · D0KWN0_HALNC
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids685 (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 | 45-49 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DAAFD | ||||||
Binding site | 95-96 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 127 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 129 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 150 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 188 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 305 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 329 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 423 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 426 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 447 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | DNA binding | |
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 > Gammaproteobacteria > Chromatiales > Halothiobacillaceae > Halothiobacillus
Accessions
- Primary accessionD0KWN0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 606-685 | BRCT | ||||
Sequence: ANALPLAGRTYVLTGTLVGMSREEAGERLKALGAKVSGSVSSKTTAVIAGSEAGSKLTKANDLGVPVLDETDLQKLLRNL |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length685
- Mass (Da)74,909
- Last updated2009-12-15 v1
- Checksum543C540751686111
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001801 EMBL· GenBank· DDBJ | ACX95027.1 EMBL· GenBank· DDBJ | Genomic DNA |