HAMAP rule MF_01125
General rule information
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Accession | MF_01125 |
Dates | 31-JAN-2004 (Created) 1-JUN-2023 (Last updated, Version 30) |
Name | Reverse_gyrase |
Scope | Bacteria
Archaea |
Templates | Q08582 (RGYR_SULAC); O29238 (RGYR_ARCFU): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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Function | Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication. |
Catalytic activity | RHEA:13065: ATP + H2O = ADP + H(+) + phosphate
EC 3.6.4.12 |
Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; | |
Subunit | Monomer. |
Domain | Both the DNA unwinding and positive supercoiling activities require the cooperation of both domains. The cooperative action between the helicase-like and the topoisomerase domains is specific. The helicase-like domain probably does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, functioning more like a protein motor. The 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and therefore 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. |
Miscellaneous | This enzyme is the only unique feature of hyperthermophilic bacteria/archaea discovered so far. It appears to be essential for adaptation to life at high temperatures. |
Similarity | In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily. |
In the C-terminal section; belongs to the prokaryotic type I/III topoisomerase family. |
Keywords
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case <FT:2> or <FT:4>
end case
Gene Ontology
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GO:0005524; Molecular function: ATP binding.
GO:0003677; Molecular function: DNA binding.
GO:0003918; Molecular function: DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity.
GO:0004386; Molecular function: helicase activity.
GO:0003677; Molecular function: DNA binding.
GO:0003918; Molecular function: DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity.
GO:0004386; Molecular function: helicase activity.
case <FT:2> or <FT:4>
GO:0008270; Molecular function: zinc ion binding.
end case
GO:0006265; Biological process: DNA topological change.
GO:0006268; Biological process: DNA unwinding involved in DNA replication.
GO:0006268; Biological process: DNA unwinding involved in DNA replication.
Cross-references
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Pfam | PF00270; DEAD; 1; |
PF01131; Topoisom_bac; 1; | |
PF01751; Toprim; 1; | |
PF00271; Helicase_C; 1; | |
PRINTS | PR00417; PRTPISMRASEI; 1; |
PROSITE | PS51192; HELICASE_ATP_BIND_1; 1; trigger=PRU00541; |
PS51194; HELICASE_CTER; 0-1; trigger=PRU00542; | |
PS50880; TOPRIM; 1; trigger=PRU00995; | |
NCBIfam | TIGR01054; rgy; 1; |
Features
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From: RGYR_PYRFU (P95479) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ZN_FING | 9 | 30 | C4-type 1 | C-x-x-C-x(10,18)-[CH]-x-x-C | ||||||||
BINDING | 106 | 113 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | x-P-x-G-x-G-K-[ST] | ||||||||
ZN_FING | 722 | 741 | C4-type 2 | C-x-x-C-x(10,18)-C-x-x-C | ||||||||
REGION | 645 | Cter | Topoisomerase I | |||||||||
ACT_SITE | 955 | 955 | For DNA cleavage activity | Y | ||||||||
BINDING | 89 | 89 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | Q |
Additional information
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Size range | 1054-1624 amino acids |
Related rules | None |
Fusion | None |
Comments | The reverse gyrases of M. jannaschii and P. horikoshii contain inteins which were excised in the alignment |