RTEL1_DROER
ID RTEL1_DROER Reviewed; 985 AA.
AC B3NSW1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Regulator of telomere elongation helicase 1 homolog {ECO:0000255|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065};
GN ORFNames=GG18780;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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.
CC {ECO:0000255|HAMAP-Rule:MF_03065}.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03065};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03065}.
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DR EMBL; CH954180; EDV45930.1; -; Genomic_DNA.
DR RefSeq; XP_001977003.1; XM_001976967.2.
DR AlphaFoldDB; B3NSW1; -.
DR SMR; B3NSW1; -.
DR STRING; 7220.FBpp0137326; -.
DR PRIDE; B3NSW1; -.
DR EnsemblMetazoa; FBtr0138834; FBpp0137326; FBgn0110988.
DR GeneID; 6550838; -.
DR KEGG; der:6550838; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; B3NSW1; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IEA:EnsemblMetazoa.
DR GO; GO:2001021; P:negative regulation of response to DNA damage stimulus; IEA:EnsemblMetazoa.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03065; RTEL1; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR030845; RTEL1.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein.
FT CHAIN 1..985
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370621"
FT DOMAIN 7..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 252..255
FT /note="DEAH box"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 173
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOD_RES 874
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 985 AA; 109689 MW; 4CEA71FB0FC9D8DB CRC64;
MPESLIAGIP VHFPFEPYPV QRAYMEKVIQ CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
RTRQSEHQQQ MVKIEKADFS GLAGGATGGE LSDLGKTMGR ANNWGVPKVI YASRTHSQLT
QAMRELKRTA YANMRSVVLG SRDQLCIHPE VMREQGNSNK TNMCKLRVHS KTCTFQMRVE
SRKDHPDLRG PSIMDIEDLV KVGQRLKICP YFASRELVPQ ADITFMPYNY LLDPKARKAN
KIELGNTIVI LDEAHNIEKI CEESASVQIK SSDVAMAIED VTHIMQVFAS GESQDMAGDE
PKDFTLDDLT LLKEMLLELE KAIDAVVVDN AAEGTTFPAS LMYELLGKAN FTYGNVATIV
SLLDKLVQYL LVASQQMSIR KGGTFTMLSD LLTIVFANKQ DVMSKVYASF KVHVQMEESK
QGHGKQQGAK QQGGWLGKGT IAAASGTSKV AKIINFWCFN PGFGMEQLLN TQVRSVILTS
GTLAPLKPLI AELAIPVAQH LENPHIVDQS QVYVKIIGTG PDRQQLISNY ANRDNPKYIS
SLGQTILNVS RIVPDGLLVF FPSYPMLNKC VDAWQASGLW ADISCKKPIF LEPRSKDQFT
STMEEFYQAI RDSKGAVFMA VCRGKVSEGL DFADRNGRAV IITGLPFPPL KDPKVILKRR
YLEANRTREN QLLSGQEWYN LDATRAVNQA IGRVIRHRND YGAILLCDSR FKDASQVQQL
SKWIRGHLGD RPQCSPFGPI VRELRQFFKN AEANMKLPDE RETDAPLETV CKTEDEPLAA
IPKLKREPGS NATFKSANES AIKVEMANSI KTWTPADYAS AAGRKLGGAA PSAMDFMSRL
DSNVSSIDFN CCTDSKSGSS DLVKIHKRER SSPTLPESSS QVSKKRYKLV ENIKVEPSSS
QAKAAPEERA DFLRALRSLV TQDQFRRFGK ALLEYKNGTY ESFQDLMAIL LDVLSAPKVR
YMLVGMRKYL KNEHKDEFDR RVGSL
