A4SYV5 · DNLJ_POLAQ
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids671 (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 | 37-41 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DIEYD | ||||||
Binding site | 86-87 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 117 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 119 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 140 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 177 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 295 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 319 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 413 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 416 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 431 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 437 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | DNA binding | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Polynucleobacter
Accessions
- Primary accessionA4SYV5
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000340365 | 1-671 | DNA ligase | |||
Sequence: MSSNSPTNLADRYAFLQAELARLEHAYYVLDNPLLPDIEYDRLYRELLDIEAAHPQWVTSESLSQRVGGTALKEFDSVTHAVPMLSLNNAFEDSELIAFDRRCREALHVEHVAYAGELKFDGLAISLRYENGTLVTAATRGDGASGEDVTANIKTIRAIPLKLTGKNIPEILEVRGEVFMYLKDFEKMNRQAAELGEKEFANPRNAAAGSLRQLDSKITAKRPLSFFAYGLGALEPQSWLPKTHEELLNAYVELGLPVCSERRVLHSVEEILAFYNEIGAKRDSLPYDIDGVVYKVNSFAEQAKLGFVSRAPRFALAHKYPAQEALTTVLGIDVQVGRTGAITPVARLAPVEVGGVTVTNATLHNEDEVKRKDVRIGDTVSVRRAGDVIPEVVSVIKERRPSDAKEFVMPSRCPVCDSHIERLADEAVARCSGGLFCGAQRKQALIHFAHRRALDIEGLGEKIVDQLVDQNLVRTPADLYRLGFTALANLERMGEKSADNLIQAINQSRNTTLARFIFALGIRHVGETTAKDLANHYQSMHALMDASVEELLTVKDVGPVVADSITSFMQEAHNREVIEQLLASGMQLSVEEKIISAAVFGKTFVLTGTFPTMTRDEAKDLLEKAGAKVAGSVSKKTDYVVAGTDAGSKLAKAEELGVPVIDEEEMLNLLK |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 594-671 | BRCT | ||||
Sequence: IISAAVFGKTFVLTGTFPTMTRDEAKDLLEKAGAKVAGSVSKKTDYVVAGTDAGSKLAKAEELGVPVIDEEEMLNLLK |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length671
- Mass (Da)73,743
- Last updated2007-05-15 v1
- Checksum27C6F953067C0E10
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000655 EMBL· GenBank· DDBJ | ABP34669.1 EMBL· GenBank· DDBJ | Genomic DNA |