F2J290 · F2J290_POLGS
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids721 (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 | 46-50 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DAEYD | ||||||
Binding site | 95-96 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 130 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 132 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 153 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 189 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 305 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 329 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 434 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 437 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 464 | 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 > Rhodobacterales > Paracoccaceae > Polymorphum
Accessions
- Primary accessionF2J290
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 | 643-716 | BRCT | ||||
Sequence: AEGSPVAGKTVVFTGALERMTRDEAKAMAERLGAKVAGSVSKKTSLVVAGPGAGSKLKTAQELDIEVITEDDWF |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length721
- Mass (Da)77,656
- Last updated2011-05-31 v1
- ChecksumD66BECB00DB35C42
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002568 EMBL· GenBank· DDBJ | ADZ69786.1 EMBL· GenBank· DDBJ | Genomic DNA |