F2KSF0 · F2KSF0_ARCVS
- ProteinReverse gyrase
- Genergy
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1069 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.
Miscellaneous
This enzyme is the only unique feature of hyperthermophilic bacteria/archaea known and seems to be essential for adaptation to life at high temperatures. It may play a role in stabilization of DNA at high temperatures.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 or 2 zinc ions per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | |
Molecular Function | reverse gyrase activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA topological change | |
Biological Process | DNA unwinding involved in DNA replication |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReverse gyrase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Archaeoglobi > Archaeoglobales > Archaeoglobaceae > Archaeoglobus
Accessions
- Primary accessionF2KSF0
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 64-249 | Helicase ATP-binding | ||||
Sequence: ARRILRGESFAAVAPTGIGKTSFGAAMALFLATKGKKSYIILPTTLLVEQVAESLAKYGEKAGVKVSLNNSDGITVLYYHGRMGKAEKEKFFELIQNADILVTTTQFLSRHFESIKRTFDFVFVDDVDAILKASRNVDRVLMLLGFRKTKKGWEGEARGVLMVSTATAKKGQKIKLFRQLLNFDVG | ||||||
Coiled coil | 398-425 | |||||
Sequence: KPEHEKELAELRKILKKLVEEGKAKEKD | ||||||
Region | 515-1069 | Topoisomerase I | ||||
Sequence: DVVKPTLFIVESPTKAKQISRFFGQPSVKAFDGIIAYEVPTAKRVLLVSASLGHVTDLITNRGFHGVEVNGHFVPVYASIKRCRQCGYQFTEERQNCPKCGSEDIDDSKRRIEALRKLAHDAGEVIIGTDPDAEGEKIAWDIQNLLAGCGEIRRAEFHEVTRRAVSEALENLRSVDENLVKAQIVRRIEDRWIGFVLSQKLWKAFGSTNLSAGRAQTPVLGWVIERAEQHREKKVIGFIRDLELSIEGLKAKKARLRIRLIEEKEEEKTPLPPYTTDAMLRDANAILKIPAKEAMAIAQTLFESGLITYHRTDSTRVSEAGMRVAREYLGEDFVAREWFAEGAHECIRPTRAVDKNTLQRLIQENVIAVEDITWRHLALYDLIFRRFMASQCKPYTVRVCRYLVEANGISVEEERVIDARGKAYELYKAVWVRKPLPEGEVEVDVEVRRVPKVPLYTQSDLIQLMREKGIGRPSTYATIIDKLFQRNYVVERNGRVMPTKRGMDVFGYLVRRYAKFVSEERTRILEEKMDAVERGELDYLKALEELYAEIKEITA | ||||||
Domain | 519-675 | Toprim | ||||
Sequence: PTLFIVESPTKAKQISRFFGQPSVKAFDGIIAYEVPTAKRVLLVSASLGHVTDLITNRGFHGVEVNGHFVPVYASIKRCRQCGYQFTEERQNCPKCGSEDIDDSKRRIEALRKLAHDAGEVIIGTDPDAEGEKIAWDIQNLLAGCGEIRRAEFHEVT | ||||||
Coiled coil | 753-780 | |||||
Sequence: IRDLELSIEGLKAKKARLRIRLIEEKEE |
Domain
Introduction of positive supercoils requires the cooperation of both domains. The helicase-like domain probably does not directly unwind DNA, but more likely acts by driving ATP-dependent conformational changes within the whole enzyme. A beta hairpin in the 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain.
Sequence similarities
In the C-terminal section; belongs to the type IA topoisomerase family.
In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,069
- Mass (Da)121,227
- Last updated2011-05-31 v1
- ChecksumC391F52B9F0CA980
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002588 EMBL· GenBank· DDBJ | AEA46919.1 EMBL· GenBank· DDBJ | Genomic DNA |