A0A2H4NRK4 · A0A2H4NRK4_AMYSP
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids589 (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 | 51-55 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DDTYD | ||||||
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 | 187 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 303 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 327 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 421 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 424 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 443 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Amycolatopsis
Accessions
- Primary accessionA0A2H4NRK4
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-457 | NAD-dependent DNA ligase N-terminal | ||||
Sequence: PSVAGYEKALAEIRAAAAAYYAGADVVMDDDTYDALLARAIATEAAHPAWKPADTPTEAVGAGVAPGTEIPHSTPMLGLDNVFDSESLRKWATRLERVLGHPVTAYTVEPKLDGLAVAARYSRGRLTLVLTRGTGTMGEDVTTRAVLAKGLPTRLSSPRTIEVRGEVFMTDEDFRTANELRTGHGEPAFAHPRSAAAGTLRAVDRAYSAPLSFTAYAVQGLADDGTHSEAMRQLEELGVATTSGGKPALKVCRSAEEIEAAVAEIRDLRGALGFGVDGAVIKADRPQDRAAAGASAKAPRWGVAVKFPADTRSTKLLAIDVQVGRTGVITPVATLEPVFIDGVKVVSATLHNFDDLQRRNVRVGDTVFVRRAGDVIPEITGAKLDERPADARPFTPPEVCPDCGSEIDRSQTRWRCTGGRTCGARKILAHYATREA | ||||||
Region | 555-589 | Disordered | ||||
Sequence: CRRSKASAGNAPRRSRASWPSWPGSSRSSRPAGSP | ||||||
Compositional bias | 573-589 | Polar residues | ||||
Sequence: WPSWPGSSRSSRPAGSP |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length589
- Mass (Da)61,877
- Last updated2018-02-28 v1
- ChecksumA51EC15C415C856A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 573-589 | Polar residues | ||||
Sequence: WPSWPGSSRSSRPAGSP |