A0A2H9QBB2 · A0A2H9QBB2_9ARCH
- ProteinDNA topoisomerase 1
- GenetopA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids754 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Catalytic activity
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 116 | Interaction with DNA | |||
Site | 228 | Interaction with DNA | |||
Site | 232 | Interaction with DNA | |||
Active site | 377 | O-(5'-phospho-DNA)-tyrosine intermediate | |||
Site | 379 | Interaction with DNA | |||
Site | 565 | Interaction with DNA | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase type I (single strand cut, ATP-independent) activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA topological change |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA topoisomerase 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Candidatus Micrarchaeota
Accessions
- Primary accessionA0A2H9QBB2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-18 | Basic and acidic residues | |||
Region | 1-60 | Disordered | |||
Compositional bias | 23-50 | Polar residues | |||
Domain | 64-203 | Toprim | |||
Region | 257-262 | Interaction with DNA | |||
Sequence similarities
Belongs to the type IA topoisomerase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length754
- Mass (Da)83,778
- Last updated2018-02-28 v1
- Checksum48B846CC94794502
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-18 | Basic and acidic residues | |||
Compositional bias | 23-50 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PFPH01000253 EMBL· GenBank· DDBJ | PIZ95710.1 EMBL· GenBank· DDBJ | Genomic DNA |