A0A085VAG6 · A0A085VAG6_PSESX
- ProteinDNA ligase (ATP)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1146 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Probably binds two magnesium or manganese ions per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 37 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 109 | |||||
Sequence: Y | ||||||
Active site | 150 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 150 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 152 | Transition state stabilizer | ||||
Sequence: N | ||||||
Site | 221 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 250 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 251 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 251 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 251 | Interaction with DNA substrate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA ligase (ATP) activity | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | double-stranded DNA 3'-5' DNA exonuclease activity | |
Molecular Function | endonuclease activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA recombination | |
Biological Process | DNA repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA ligase (ATP)
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A085VAG6
Proteomes
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 262-285 | Disordered | ||||
Sequence: HAKRKKTSTKAEHPSAGSAAHSNL | ||||||
Region | 293-312 | Disordered | ||||
Sequence: NFDATPEPSGATSTKGSGKQ | ||||||
Compositional bias | 298-312 | Polar residues | ||||
Sequence: PEPSGATSTKGSGKQ | ||||||
Domain | 604-742 | ATP-dependent DNA ligase family profile | ||||
Sequence: EVGRSGNIVYYLFDLPFLNGMDLREVRVEQRRAALSKALEASEDEILRFSEDFGEEPDALLNSACQMKMEGLIGKRVGSSYVSRRSGDWIKLKCKRRQEFVVVGFSEPKGARSKFGALLLGLHDADSGDLRYAGKVGTG | ||||||
Region | 826-853 | Disordered | ||||
Sequence: IGKPTKRPRQPVKATTTKGAVGAAATPA |
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,146
- Mass (Da)127,957
- Last updated2014-10-29 v1
- Checksum7A4636643C753581
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 298-312 | Polar residues | ||||
Sequence: PEPSGATSTKGSGKQ |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JPQT01000097 EMBL· GenBank· DDBJ | KFE52429.1 EMBL· GenBank· DDBJ | Genomic DNA |