A0A292Z1H4 · A0A292Z1H4_9PSEU
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids802 (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: DGQFD | ||||||
Binding site | 95-96 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 125 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 127 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 148 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 188 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 304 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 328 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 422 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 425 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 441 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 447 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Pseudonocardia
Accessions
- Primary accessionA0A292Z1H4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MSTDSPAGTAPRPAPDADRE | ||||||
Region | 570-631 | Disordered | ||||
Sequence: TAKAGVEITSDGSSDEPDADFVPDVDSVPDAVEEPDAVEEPDAVEEPAAAGDSGAGDSGADA | ||||||
Compositional bias | 582-615 | Acidic residues | ||||
Sequence: SSDEPDADFVPDVDSVPDAVEEPDAVEEPDAVEE | ||||||
Domain | 709-781 | BRCT | ||||
Sequence: SIPRTLDGLSIVITGSMAGWSRDEAKEAIAARGGRAAGSVSKKTAFLVAGDAPGSKYDKALELGVPILDEAGL |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length802
- Mass (Da)85,794
- Last updated2017-12-20 v1
- ChecksumBD2EF7A684395D02
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 582-615 | Acidic residues | ||||
Sequence: SSDEPDADFVPDVDSVPDAVEEPDAVEEPDAVEE |