ID   RTEL1_DROPS             Reviewed;        1009 AA.
AC   Q29FS3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 82.
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=GA17940;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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; CH379065; EAL31506.2; -; Genomic_DNA.
DR   RefSeq; XP_001354453.2; XM_001354417.3.
DR   AlphaFoldDB; Q29FS3; -.
DR   SMR; Q29FS3; -.
DR   STRING; 7237.FBpp0272129; -.
DR   EnsemblMetazoa; FBtr0273691; FBpp0272129; FBgn0077949.
DR   GeneID; 4814338; -.
DR   KEGG; dpo:Dpse_GA17940; -.
DR   eggNOG; KOG1132; Eukaryota.
DR   HOGENOM; CLU_006515_4_0_1; -.
DR   InParanoid; Q29FS3; -.
DR   OMA; GNCATIV; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0077949; Expressed in female reproductive system and 3 other tissues.
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   Reference proteome.
FT   CHAIN           1..1009
FT                   /note="Regulator of telomere elongation helicase 1 homolog"
FT                   /id="PRO_0000370626"
FT   DOMAIN          7..322
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"
SQ   SEQUENCE   1009 AA;  112164 MW;  F4A06894F01B09E3 CRC64;
     MPESVIAGIP VHFPFEPYNV QRDYMEKVII CLRDGTNGVL ESPTGTGKTL SLLCASLAWI
     RTRQSEHQQQ MIKLKATSKE GGPGSGPGGD LSELAMTVGQ ANNWGVPKVI YASRTHSQLN
     QAMRELKRTA YANMRSVVLG SRDQLCIHPE VMKEQGNSNK VNLCKLRVHS KTCTFQLRVE
     SKKDHPDFRG PSIMDIEDLV RVGQKLKMCP YYASKELVAQ ADITFMPYNY LLDPKARKAN
     KIELGNTIII LDEAHNIEKI CEESASVQIR SSDVAMAIED VTHIMKVFTS GESQEAGGDE
     PKDFTLDDLT LLKEMLLELE KAIDAVVVDN PTDGTTYPAS LMYELLGKAN FTYGNCATIV
     ALLDKLVQYL MVASQHMTIR KGGTFTMLSD LLTIVFANKE NIMSKVHLSF KVHVQVEESN
     KQQGKSGATQ GKQQGWLGKG NITTTGTSSK AAKIVNFWCF NPGFGMEQLL NTQVRSVILT
     SGTLAPLKPL IAELAIPVAQ HLENPHIVDQ SQVYVKIIGT GPDRQQLISN FKNRDNPKYI
     SSLGQTILNV ARIVPDGLLV FFPSYPMLNK CVDAWQASGL WADISCKKPI FVEPRGKDQF
     TSTMEEFYQA IRDSKGAVFM AVCRGKVSEG LDFADRNGRA VIITGLPFPP LKDPKVILKR
     RYLETNRTKE NQLLSGQEWY NLDATRAVNQ AIGRVIRHRN DYGAILLCDS RFQDASQVQQ
     LSKWIRGHLG ARPQSSPFGP IVRELRQFFK HAEETMKQPD VREEEQPLMN VCKVEEVGTL
     PVIPTIKQEP GNNATFRKAN KSAIKVEMAN SINSWTPADY ASAAGRTLGK AAPNAMDFMS
     RLDSNVSSID FNCSGSADSG SGGCGSSSLV TIHKRERSSP GVTDTVATQT TKKRYKLAEN
     IKTEPKSNSS QQVKVAPESR ADFLRELRSL ISQDQFRDFG KVLIEYRSGT DENFESLMTV
     LLDVLAAPKM RYLFIGMRRF LRNEHKAEFD VRLASLNLAQ ESSPNKRIP