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Annotation rule MF_01125
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General rule information [?]

Accession MF_01125
Dates 31-JAN-2004 (Created)
21-JAN-2019 (Last updated, Version 23)
Name Reverse_gyrase
Scope
Bacteria
Archaea
Templates Q08582 (RGYR_SULAC); O29238 (RGYR_ARCFU): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
RGYR
Protein name
RecName: Full=Reverse gyrase;
Includes:
RecName: Full=Helicase;
EC=3.6.4.12;
Includes:
RecName: Full=Topoisomerase;
EC=5.6.2.3;
Gene name
rgy

Comments [?]

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 Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;.
Reaction=ATP-dependent breakage, passage and rejoining of double- stranded DNA.; EC=5.6.2.3;.
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 [?]

Hydrolase
Isomerase
Topoisomerase
Helicase
DNA-binding
ATP-binding
Nucleotide-binding
case <FT:2> or <FT:4>
Metal-binding
Zinc
Zinc-finger
end case

Gene Ontology [?]

GO:0005524; Molecular function: ATP binding.
GO:0003677; Molecular function: DNA binding.
GO:0003918; Molecular function: DNA topoisomerase type II (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.

Cross-references [?]

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;
TIGRFAMs TIGR01054; rgy; 1;

Features [?]

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  
NP_BIND     106     113       ATP     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       ATP     Q  

Additional information [?]

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


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