HAMAP rule MF_03065
General rule information
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Accession | MF_03065 |
Dates | 23-JAN-2014 (Created) 1-JUN-2023 (Last updated, Version 10) |
Name | RTEL1 |
Scope | Eukaryota; Metazoa |
Templates | Q9NZ71 (RTEL1_HUMAN); Q0VGM9 (RTEL1_MOUSE); Q93575 (RTEL1_CAEEL): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
case <OC:Vertebrata>
Protein name |
|
else
Protein name |
|
end case
case <OC:Vertebrata>
Gene name |
|
else case <OC:Caenorhabditis>
Gene name |
|
end case
Comments
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case <OC:Vertebrata>
Function | ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere. |
else
Function | ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. |
end case
Catalytic activity | RHEA:13065: ATP + H2O = ADP + H(+) + phosphate
EC 3.6.4.12 |
case <OC:Mammalia>
Subunit | Interacts with TERF1. Interacts (via PIP-box) with PCNA; the interaction is direct and essential for suppressing telomere fragility. Interacts with MMS19; the interaction mediates the association of RTEL1 with the cytosolic iron-sulfur protein assembly (CIA) complex. |
end case
case <OC:Mammalia>
Subcellular location | Nucleus. Note=Colocalizes with PCNA within the replication foci in S-phase cells. |
else
Subcellular location | Nucleus. |
end case
case <FTTag:PIP>
Domain | The PIP-box (PCNA interacting peptide) motif mediates the interaction with PCNA and localization to replication foci. |
end case
Similarity | Belongs to the helicase family. RAD3/XPD subfamily. |
Keywords
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case <FTGroup:1>
end case
Gene Ontology
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GO:0005634; Cellular component: nucleus.
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
GO:0005524; Molecular function: ATP binding.
GO:0003678; Molecular function: DNA helicase activity.
GO:0003677; Molecular function: DNA binding.
GO:0046872; Molecular function: metal ion binding.
GO:0006281; Biological process: DNA repair.
GO:0010569; Biological process: regulation of double-strand break repair via homologous recombination.
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
GO:0005524; Molecular function: ATP binding.
GO:0003678; Molecular function: DNA helicase activity.
GO:0003677; Molecular function: DNA binding.
GO:0046872; Molecular function: metal ion binding.
GO:0006281; Biological process: DNA repair.
GO:0010569; Biological process: regulation of double-strand break repair via homologous recombination.
case <OC:Vertebrata>
GO:0000723; Biological process: telomere maintenance.
end case
Cross-references
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PROSITE | PS51193; HELICASE_ATP_BIND_2; 1; trigger=PRU00541; |
PS00690; DEAH_ATP_HELICASE; 1; | |
Pfam | PF06733; DEAD_2; 1; |
PF13307; Helicase_C_2; 1; | |
NCBIfam | TIGR00604; rad3; 1; |
Features
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case <OC:Vertebrata>
From: RTEL1_HUMAN (Q9NZ71) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
MOTIF | 151 | 167 | Nuclear localization signal | [RK]-[RK]-x(11)-R-[RK]-K-x | ||||||||
MOTIF | 871 | 877 | Nuclear localization signal | x(4)-[RK]-[RK]-K |
end case
case <OC:Mammalia>
end case
Additional information
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Size range | 783-1334 amino acids |
Related rules | None |
Fusion | None |