We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU01380
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01380
General rule information
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| Accession | PRU01380 |
| Dates | 13-SEP-2023 (Created)
13-SEP-2023 (Last updated, Version 2) |
| Data class | Domain; |
| Predictors |
PROSITE; PS52036; ZF_RG_N |
Name | Zinc finger reverse gyrase N-terminal-type |
| Function | Reverse gyrase (RG) is an ATP-dependent topoisomerase that is only found in archaeal and bacterial hyperthermophiles (above 80 degre C) and thermophiles (65-80 degre C). RGs share a modular structure with an N- terminal cysteine-rich region (a zinc finger) preceding a helicase domain that is followed by a C-terminal topoisomerase domain. The helicase domain is subdivided into H1 and H2 domains that are flexibly linked. Some RG topoisomerase domains also include a cysteine-rich region that has been proposed to form a second zinc finger. The two zinc-finger motifs are found to be important to the structure stability maintenance of RG at high temperature. The N-terminal zinc finger firmly attaches the H1 domain to the topoisomerase domain and may contribute to double-strand DNA (dsDNA) binding. |
| Scope(s) |
Archaea Bacteria |
| Example(s) | P0DW67; |
Propagated annotation
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Comments
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| case (<Feature:PS52036:11=[CH]> and <Feature:PS52036:14=[CH]> and <Feature:PS52036:29=[CH]> and <Feature:PS52036:32=[CH]>) | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; |
Keywords
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| Metal-binding | |
| Zinc | |
| end case | |
| Zinc-finger | |
Gene Ontology
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| GO:0046872; Molecular function:metal ion binding |
| GO:0008270; Molecular function:zinc ion binding |
Features
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| From: PS52036 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case (<Feature:PS52036:11=[C]> and <Feature:PS52036:14=[C]> and <Feature:PS52036:29=[C]> and <Feature:PS52036:32=[C]>) | ||||||||||||
| ZN_FING | from | to | /note="RG N-terminal-type #" | |||||||||
| else case (<Feature:PS52036:11=[CH]> and <Feature:PS52036:14=[CH]> and <Feature:PS52036:29=[CH]> and <Feature:PS52036:32=[CH]>) | ||||||||||||
| ZN_FING | from | to | /note="RG N-terminal-type #; atypical" | |||||||||
| else | ||||||||||||
| ZN_FING | from | to | /note="RG N-terminal-type #; degenerate" | |||||||||
| end case | ||||||||||||
| BINDING | 11 | 11 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" |
[CH] | 1 | |||||||
| BINDING | 14 | 14 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" |
[CH] | 1 | |||||||
| BINDING | 29 | 29 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" |
[CH] | 1 | |||||||
| BINDING | 32 | 32 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" |
[CH] | 1 | |||||||
Additional information
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| Size range | 37-47 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Archaea [18] Bacteria [4] All [ 22 ]
- Retrieve set of proteins with 3D structure for this domain