ProRule PRU01364
General rule information
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| Accession | PRU01364 |
| Dates | 17-MAR-2023 (Created)
-- (Last updated, Version 1) |
| Data class | Domain; |
| Predictors |
PROSITE; PS52020; CRESS_DNA_REP |
Name | CRESS-DNA virus replication initiator protein (Rep) endonuclease domain |
| Function | The Rep endonuclease domain is characterized by rolling circle replication (RCR) motifs I through III, which are important for RCR initiation and termination. Motif I, UUTU (U denotes hydrophobic residues), is thought to be involved in the recognition of the origin of replication. Motif II, HU(H/Q), is involved in the coordination of divalent metal ions, Mg(2+) or Mn(2+), which are essential for endonuclease activity at the origin of replication. Motif III (YxxK, where x is any amino acid) is involved in dsDNA cleavage and subsequent covalent attachment of the Rep through the catalytic tyrosine residue to the 5' end of the cleaved product. |
| Scope(s) |
Viruses Cressdnaviricota Bacteria Candidatus Phytoplasma asteris |
| Example(s) | D4N3P2 (REP_HCYV5); |
Propagated annotation
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Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). |
| end case | |
| SUBCELLULAR LOCATION | Host nucleus. |
Keywords
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| DNA-binding | |
| Host nucleus | |
| DNA replication | |
| Nucleotide-binding | |
| case <FTTag:act_site> | |
| Endonuclease | |
| Hydrolase | |
| Nuclease | |
| Covalent protein-DNA linkage | |
| Nucleotidyltransferase | |
| Transferase | |
| end case | |
| case <FTGroup:1> | |
| Metal-binding | |
| end case | |
Gene Ontology
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| GO:0006260; Biological process:DNA replication | |
| GO:0003677; Molecular function:DNA binding | |
| GO:0042025; Cellular component:host cell nucleus | |
| case <FTGroup:1> | |
| GO:0046872; Molecular function:metal ion binding | |
| end case | |
| case <FTTag:act_site> | |
| GO:0016888; Molecular function:endodeoxyribonuclease activity, producing 5'-phosphomonoesters | |
| GO:0016779; Molecular function:nucleotidyltransferase activity | |
| end case | |
Features
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| From: PS52020 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="CRESS-DNA virus Rep endonuclease #" | |||||||||
| MOTIF | 8 | 11 | /note="RCR-1" | [FWILMVACGTSYPH](2)-T-[FWILMVACGTSYPH] | ||||||||
| MOTIF | 47 | 49 | /note="RCR-2" | H-[FWILMVACGTSYPH]-[HQ] | ||||||||
| MOTIF | 87 | 90 | /note="RCR-3" | Y-x(2)-K | ||||||||
| ACT_SITE | 87 | 87 | /note="For DNA cleavage activity" | act_site | Y | |||||||
| BINDING | 39 | 39 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
E | 1 | |||||||
| BINDING | 47 | 47 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
H | 1 | |||||||
| BINDING | 49 | 49 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
H | 1 | |||||||
| BINDING | 91 | 91 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
[DEN] | 1 | |||||||
Additional information
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| Size range | 94-130 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
Bacteria [1] Viruses [73] All [ 74 ]
- Retrieve set of proteins with 3D structure for this domain