P35970 · DNLI_ASFB7
- ProteinDNA ligase
- GeneLIG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Very low-fidelity DNA ligase that seals nicks in double-stranded DNA during DNA repair (PubMed:15938630).
Together with the viral repair DNA polymerase X, fills the single nucleotide gaps generated by the AP endonuclease (PubMed:15938630).
It is not essential for viral replication and recombination (PubMed:15938630).
Displays a very low adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-terminated nicks compared to regular nick DNA (PubMed:15938630).
Together with the viral repair DNA polymerase X, fills the single nucleotide gaps generated by the AP endonuclease (PubMed:15938630).
It is not essential for viral replication and recombination (PubMed:15938630).
Displays a very low adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-terminated nicks compared to regular nick DNA (PubMed:15938630).
Miscellaneous
Consistent with its intracellular location, ASFV encodes its own replicative DNA polymerase and three base excision repair enzymes: a class II AP endonuclease, the repair polymerase Pol X, and an ATP-dependent DNA ligase.
Catalytic activity
Cofactor
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 149 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 151 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 151 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 153 | Important for the catalytic efficiency | ||||
Sequence: N | ||||||
Binding site | 203 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 203 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 211 | Important for the catalytic efficiency | ||||
Sequence: L | ||||||
Binding site | 232 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 291 | a divalent metal cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 294 | ATP (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 316 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 402 | Important for the catalytic efficiency | ||||
Sequence: L | ||||||
Site | 403 | Important for the catalytic efficiency | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | virion component | |
Molecular Function | ATP binding | |
Molecular Function | DNA ligase (ATP) activity | |
Molecular Function | metal ion binding | |
Biological Process | cell division | |
Biological Process | DNA recombination | |
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
- Taxonomic lineageViruses > Varidnaviria > Bamfordvirae > Nucleocytoviricota > Pokkesviricetes > Asfuvirales > Asfarviridae > Asfivirus > African swine fever virus
- Virus hosts
Accessions
- Primary accessionP35970
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in association with the viral nucleoid.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059592 | 1-419 | DNA ligase | |||
Sequence: MLNQFPGQYSNNIFCFPPIESETKSGKKASWIICVQVVQHNTIIPITDEMFSTDVKDAVAEIFTKFFVEEGAVRISKMTRVTEGKNLGKKNATTVVHQAFKDALSKYNRHARQKRGAHTNRGMIPPMLVKYFNIIPKTFFEEETDPIVQRKRNGVRAVACQQGDGCILLYSRTEKEFLGLDNIKKELKQLYLFIDVRVYLDGELYLHRKPLQWIAGQANAKTDSSELHFYVFDCFWSDQLQMPSNKRQQLLTNIFKQKEDLTFIHQVENFSVKNVDEALRLKAQFIKEGYEGAIVRNANGPYEPGYNNYHSAHLAKLKPLLDAEFILVDYTQGKKGKDLGAILWVCELPNKKRFVVTPKHLTYADRYALFQKLTPALFKKHLYGKELTVEYAELSPKTGIPLQARAVGFREPINVLEII |
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-120 | NTD | ||||
Sequence: MLNQFPGQYSNNIFCFPPIESETKSGKKASWIICVQVVQHNTIIPITDEMFSTDVKDAVAEIFTKFFVEEGAVRISKMTRVTEGKNLGKKNATTVVHQAFKDALSKYNRHARQKRGAHTN | ||||||
Region | 121-317 | AD domain | ||||
Sequence: RGMIPPMLVKYFNIIPKTFFEEETDPIVQRKRNGVRAVACQQGDGCILLYSRTEKEFLGLDNIKKELKQLYLFIDVRVYLDGELYLHRKPLQWIAGQANAKTDSSELHFYVFDCFWSDQLQMPSNKRQQLLTNIFKQKEDLTFIHQVENFSVKNVDEALRLKAQFIKEGYEGAIVRNANGPYEPGYNNYHSAHLAKL | ||||||
Region | 318-419 | OB domain | ||||
Sequence: KPLLDAEFILVDYTQGKKGKDLGAILWVCELPNKKRFVVTPKHLTYADRYALFQKLTPALFKKHLYGKELTVEYAELSPKTGIPLQARAVGFREPINVLEII |
Domain
The N-terminus domain (NTD) plays a critical role in DNA-binding, catalytic complex assembly and catalysis.
Sequence similarities
Belongs to the ATP-dependent DNA ligase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)48,164
- Last updated1994-06-01 v1
- Checksum491A25A4B9CFD807
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X65373 EMBL· GenBank· DDBJ | CAA46445.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18466 EMBL· GenBank· DDBJ | AAA65329.1 EMBL· GenBank· DDBJ | Genomic DNA |