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RTEL1_DROGR
ID   RTEL1_DROGR             Reviewed;         986 AA.
AC   B4JNS2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=GH24089;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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; CH916371; EDV92365.1; -; Genomic_DNA.
DR   RefSeq; XP_001992658.1; XM_001992622.1.
DR   AlphaFoldDB; B4JNS2; -.
DR   SMR; B4JNS2; -.
DR   STRING; 7222.FBpp0157995; -.
DR   PRIDE; B4JNS2; -.
DR   eggNOG; KOG1132; Eukaryota.
DR   HOGENOM; CLU_006515_4_0_1; -.
DR   InParanoid; B4JNS2; -.
DR   OMA; GNCATIV; -.
DR   PhylomeDB; B4JNS2; -.
DR   Proteomes; UP000001070; 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; Reference proteome.
FT   CHAIN           1..986
FT                   /note="Regulator of telomere elongation helicase 1 homolog"
FT                   /id="PRO_0000370622"
FT   DOMAIN          7..326
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   MOTIF           254..257
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         148
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         166
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         175
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         211
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   MOD_RES         875
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   986 AA;  109960 MW;  1107B6A97E125818 CRC64;
     MPENIIAGIP VHFPFEPYDV QRAYMEKVII CLRDGTNGVL ESPTGTGKTL SLLCSTLGWI
     RTRQSEVQLN MQKLQHDQQT QLTGAAGAGA AMGSEIAAVI GKSNNWGVPK VIYASRTHSQ
     LTQAMRELKR TAYANMRAVV LGSRDQLCIH PDVMREQGNS NKVNMCKLKV HAKSCTFQLR
     VESKKDHPDF RGPSIMDIED LVKVGQRLKM CPYFASKELV NSADITFMPY NYLLDPKARK
     ANKIELSNAI VILDEGHNIE KICEESASVQ IRSSDVAIAI EDVTHIMKIF TSSSDSQDTA
     GPDEPKDFTI DDLTLLKEML LELEKAIDGV IVDNKADGAT YPASYMYELL GKANFTHGNC
     ATIVALLDKL VQYLMVASQH SMLRKGGSFM VLADLLNIVF ANKGDIMSKV SCSFKVHAEI
     EESKQSQTNN KAQTGWLGKG NNNAASSASK TGRIINFWCF NPGFGMEQLL NTHVRSVILT
     SGTLAPLKPL IAELAIPVAQ HLENPHIVNE AQVYVKIIGT GPDREQLISN YKNRDNPKYI
     SSLGQTILNV SRIVPDGLLV FFPSYPMLNQ CVDAWQASGL WADISSRKPI FLEPRGKDQF
     TSTMEEFYQA IRDSKGACFM AVCRGKVSEG LDFADRNGRA VIITGLPFPP LKDPKVILKR
     RYLETNRTRE NQLLSGNEWY NLEATRAVNQ AIGRVIRHRN DYGAILLCDA RFQDASQVQQ
     LSKWIRNHLG ARPQSSPFGP IVRELRQFFK HAEQTIVQPV ERAVEPVLHT ICSKKEDQLT
     LAPITQIKRE PGNTGTSKFQ LASELAAKVE MANSIKTWTP ADYANAAGRN AQSPKAPNPM
     DFMSRLNSNV TSIDFNADSG RDLVKIHKRE RSSPTFHNES MGSKKRYRLI NNIAQSELKE
     APESRADFLR EVRSVINSDQ FRSFGKALLA YKTGGDDSFE TLMLLLLDVM GAPKLRYLLH
     GMRRYLKNEH KSEFDVRLAS LEAAQL
 
 
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