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RTEL1_DROSE
ID   RTEL1_DROSE             Reviewed;         966 AA.
AC   B4I0K4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=GM12432;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480819; EDW53035.1; -; Genomic_DNA.
DR   RefSeq; XP_002036876.1; XM_002036840.1.
DR   AlphaFoldDB; B4I0K4; -.
DR   SMR; B4I0K4; -.
DR   STRING; 7238.B4I0K4; -.
DR   EnsemblMetazoa; FBtr0195417; FBpp0193909; FBgn0167369.
DR   HOGENOM; CLU_006515_4_0_1; -.
DR   OMA; GNCATIV; -.
DR   PhylomeDB; B4I0K4; -.
DR   Proteomes; UP000001292; 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..966
FT                   /note="Regulator of telomere elongation helicase 1 homolog"
FT                   /id="PRO_0000370627"
FT   DOMAIN          7..284
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   REGION          844..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           233..236
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         855
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   966 AA;  107500 MW;  A36C0CB89EFA78D4 CRC64;
     MPESLIAGIP VHFPFEPYPV QRAYMEKVIH CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
     RTRQSEHQMQ MVKMEKADFS GIGGGAPGGD LSELAKTMGR ANNWGVPKVI YASRTHSQLT
     QAMRELKRTA YANMRSVVLG SRDQLCIHPE VMRELGNSNK TNMCKLRVHS KTCSFQMRVE
     SRKDHPDLRG PTIMDIEDLV KVGQRLKICP YFASRELARA NKIELGNTIV ILDEAHNIEK
     ICEEYASVQI KSSDVAMTIE DITHIRQVFA SGESQDMAGD EPKDFTLDDL TLLKEMLLEL
     EKAIDAVVVD NAVDGTTFPA SMMYELLGKA NFTYGNVASI ISLLDKLVQY LLVASQQMSI
     RKGGTFTLLS DLLTIVFANK EDVMSKVYAS FKVHVLVEES KQGHGKQQGA KQQGGWLGKG
     TIAAATGSSK VAKIINFWCF NPGFGMEQLL NTQVRSVILT SGTLAPLKPL IAELAIPVAQ
     HLENPHIVDQ SQVYVKIIGT GPDRQQLISN YANRDNPKYV SSLGQTILNV ARIVPDGLLV
     FFPSYPMLNK CVDAWQASGL WADISCKKPI FLEPRSKDQF TSTMEEFYQA IRDSKGAVFM
     AVCRGKVSEG LDFADRNGRA VIITGLPFPP LKDPKVILKR RYLEANRTRE NQLLSGQEWY
     NLDATRAVNQ AIGRVIRHRN DYGAILLCDS RFKDASQVQQ LSKWIRGHLG DRPQCSPFGP
     IVRELRQFFK NAEANMKLPD ERETDSPLET VCKTEVEPLA AIPKVKREPG SNATFKSANE
     SAIKVEMANS IKTWTPADYA SAAGRKLGGA APNAMDFMSR LDSNVSSIDF NCCTDSKSGS
     SGLVKIHKRE RSSPTAPEST SQVSKKRYKL VENIKVEPSS SQAKVAPEDR AAFLRELRSL
     VTQDQFRRFG KALLEYKNGT YESFQALMAI LLDVLSAPKV RYMLVGMRKY LKNEHKEEFD
     RRVGNL
 
 
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