RTEL1_DROYA
ID RTEL1_DROYA Reviewed; 985 AA.
AC B4PZB4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=GE16425;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000162; EDX01081.1; -; Genomic_DNA.
DR RefSeq; XP_002099973.1; XM_002099937.2.
DR AlphaFoldDB; B4PZB4; -.
DR SMR; B4PZB4; -.
DR STRING; 7245.FBpp0261435; -.
DR EnsemblMetazoa; FBtr0262943; FBpp0261435; FBgn0233951.
DR GeneID; 6524109; -.
DR KEGG; dya:Dyak_GE16425; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; B4PZB4; -.
DR Proteomes; UP000002282; Chromosome X.
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_0000370630"
FT DOMAIN 7..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 858..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 109872 MW; 2E08CF4319C006E0 CRC64;
MPESLIAGIP VHFPFEPYPV QRAYMEKVIQ CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
RTRQSEHQQQ MVKMEKADFT GLGGGAAGGD LSELAKTMGR ANNWGVPKVI YASRTHSQLT
QAMRELKRTA YANMRSVVLG SRDQLCIHPE VMREQGNSNK TNMCKLRVHS KTCSFQMRVE
SRKDHPDLRG PSIMDIEDLV KVGQRLKICP YFASRELVPQ ADITFMPYNY LLDPKARKAN
KIELGNTIVI LDEAHNIEKI CEESASVQIK SSDVAMAIED VTHIMQVFAS GESQDMGGDE
PKDFTLDDLT LLKEMLLEFE KAIDAVVVEN AVEGTTFPAS MMYELLGKAN FTYGNVATIV
SLLDKLVQYL LVASQQMTIR KGGTFTMLSD LLTIVFANKE DVMSKVYASF KVHVQLEEVK
QGHGKQQGGK QHGGWLGKGT IAAATGSIKV AKIINFWCFN PGFGMEQLLN TQVRSVILTS
GTLAPLKPLI AELAIPVAQH LENPHIVDQS QVYVKIIGTG PDRQQLISNY ANRDNPKYIS
SLGQTILNVS RIVPDGLLVF FPSYPMLNKC VDAWQASGLW ADISVKKPIF LEPRSKDQFT
STMEEFYQAI RDSKGAVFMA VCRGKVSEGL DFADRNGRAV IITGLPFPPL KDPKVILKRR
YLEANRTREN QLLSGQEWYN LDATRAVNQA IGRVIRHRND YGAILLCDSR FKDASQVQQL
SKWIRGHLGD RPQCSPFGPI VRELRQFFKN AEANMKLPDE RETDSPLETV CKTENEPIAA
IPKVKREPGS NATFKSANES AIKVEMANSI KTWTPADYAS AAGRKLGGAA PNAMDFMSRL
DSNVSSIDFN CCMDSKSGSS GMVKIHKRER SSPTQPESSS QVSKKRYKLV ENIKVEPSSS
QVKEAPAERA DFLRELRSLV TQDQFRRFGK ALLEYKDGTY ESFQALMVIL LDVLSAPKVR
YMLVGMRKYL KNEHKDEFDQ KVGKL
