AC MF_03065; DC Protein; auto TR HAMAP; MF_03065; -; 1; level=0 XX Names: RTEL1 XX ID RTEL1 case DE RecName: Full=Regulator of telomere elongation helicase 1; DE EC=3.6.4.12; else DE RecName: Full=Regulator of telomere elongation helicase 1 homolog; DE EC=3.6.4.12; end case case GN Name=RTEL1; else case GN Name=rtel-1; Synonyms=bch-1; end case XX case CC -!- FUNCTION: ATP-dependent DNA helicase implicated in telomere-length CC regulation, DNA repair and the maintenance of genomic stability. Acts CC as an anti-recombinase to counteract toxic recombination and limit CC crossover during meiosis. Regulates meiotic recombination and crossover CC homeostasis by physically dissociating strand invasion events and CC thereby promotes noncrossover repair by meiotic synthesis dependent CC strand annealing (SDSA) as well as disassembly of D loop recombination CC intermediates. Also disassembles T loops and prevents telomere CC fragility by counteracting telomeric G4-DNA structures, which together CC ensure the dynamics and stability of the telomere. else CC -!- FUNCTION: ATP-dependent DNA helicase implicated in DNA repair and the CC maintenance of genomic stability. Acts as an anti-recombinase to CC counteract toxic recombination and limit crossover during meiosis. CC Regulates meiotic recombination and crossover homeostasis by physically CC dissociating strand invasion events and thereby promotes noncrossover CC repair by meiotic synthesis dependent strand annealing (SDSA) as well CC as disassembly of D loop recombination intermediates. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; case CC -!- SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; the CC interaction is direct and essential for suppressing telomere fragility. CC Interacts with MMS19; the interaction mediates the association of RTEL1 CC with the cytosolic iron-sulfur protein assembly (CIA) complex. end case case CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with PCNA within the CC replication foci in S-phase cells. else CC -!- SUBCELLULAR LOCATION: Nucleus. end case case CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the CC interaction with PCNA and localization to replication foci. end case CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily. XX DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1; trigger=yes DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1; trigger=no DR Pfam; PF06733; DEAD_2; 1; trigger=no DR Pfam; PF13307; Helicase_C_2; 1; trigger=no DR NCBIfam; TIGR00604; rad3; 1; trigger=no XX KW ATP-binding KW DNA damage KW DNA repair KW DNA-binding KW Helicase KW Hydrolase KW Nucleotide-binding KW Nucleus case KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding end case XX GO GO:0005634; C:nucleus GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0005524; F:ATP binding GO GO:0003678; F:DNA helicase activity GO GO:0003677; F:DNA binding GO GO:0046872; F:metal ion binding GO GO:0006281; P:DNA repair GO GO:0010569; P:regulation of double-strand break repair via homologous recombination case GO GO:0000723; P:telomere maintenance end case XX FT From: RTEL1_HUMAN (Q9NZ71) case FT MOTIF 151..167 FT /note="Nuclear localization signal" FT Condition: [RK]-[RK]-x(11)-R-[RK]-K-x FT MOTIF 871..877 FT /note="Nuclear localization signal" FT Condition: x(4)-[RK]-[RK]-K end case case FT MOTIF 1178..1185 FT /note="PIP-box" FT Tag: PIP; Condition: Q-x(2)-[ILVAMG]-x(2)-[FL]-[FL] end case FT BINDING 145 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 163 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 172 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 207 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C XX Size: 783-1334; Related: None; Template: Q9NZ71; Q0VGM9; Q93575; Scope: Eukaryota; Metazoa Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.10 2023/06/01 //