RTEL1_DROMO
ID RTEL1_DROMO Reviewed; 1014 AA.
AC B4L1Z2;
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=GI15901;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933810; EDW07713.1; -; Genomic_DNA.
DR RefSeq; XP_002010396.1; XM_002010360.2.
DR AlphaFoldDB; B4L1Z2; -.
DR SMR; B4L1Z2; -.
DR STRING; 7230.FBpp0165118; -.
DR EnsemblMetazoa; FBtr0166626; FBpp0165118; FBgn0138650.
DR GeneID; 6584754; -.
DR KEGG; dmo:Dmoj_GI15901; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; B4L1Z2; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; B4L1Z2; -.
DR Proteomes; UP000009192; 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..1014
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370624"
FT DOMAIN 7..324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 891..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 253..256
FT /note="DEAH box"
FT COMPBIAS 893..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 165
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 174
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOD_RES 873
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1014 AA; 113029 MW; 9FE97B8B3A7E2808 CRC64;
MPESIIAGIP VHFPFEPYEV QRAFMEKVIM CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
RTRQSEHQIN MQKLQMEQQQ RQATGGSATG AISDLALTMG KANNWGVPKV IYASRTHSQL
TQAMRELKRT AYASMRSVVL GSRDQLCIHP DVMKEQGNSN KVNMCKLKVH AKTCSFQLRV
ESKKDHPDFR GPSIMDIEDL VKVGQRLKMC PYYASKELVS SADITFMPYN YLLDPKARKA
NKIELSNTIV ILDEAHNIEK ICEESASVQI RSSDVAMAIE DVTHIMKIFT SADSQDSGGP
EEPKDFTLDD LTLLKEMLLE LEKAIDGVVV ENQVEGTTYP AAHIYELLGK ANFTYGNCAT
IVALLDKLVQ YLMVASQHSM LRKGGSFMVL SDLLNVVFAN KEDIMAKVHR SFKVHVQIED
TKQTKPAGNS NSKQTGWLGK GNNATSTVSK TAKIINFWCF NPGFGMEQLL NTQVRSVILT
SGTLAPLKPL IAELAIPVAQ HLENPHIVDQ SQVYVKIIGT GPDREQLISN YKNRDNPKYI
SSLGQTILNV SRIVPDGLLV FFPSYPMLNQ CVDAWQASGL WADLSSRKPI FLEPRGKDQF
TSTMEEFYQA IRDSKGACFM AVCRGKVSEG LDFADRNGRA VIITGLPFPP LKDPKVILKR
RYLETNRTKE NQLLSGQEWY NLDATRAVNQ AIGRVIRHRH DYGAILLCDA RFQDASQVQQ
LSKWIRGHLG ARPQSSPFGP IVRELRQFFK HAEQTMVQPD ERVVEPPLQI VCKEEQPTLT
PSYNSNTQIK REPGSGVNKF QLASELAAKA EMANSIKSWT PADYVNAAGC TNQSQTAPNA
MDFMSRLNSN VTSIDFNNTD LVKIHKRERS SPTANESLTS GKKRFKLISS TDMVKTEPGT
SNSCSYGNTS SSGSDSRCCS AKPAEYPLKE APESRADFLR EVRSVVDSDK FRSFGKALLA
YKTGGDNCFE VLMVLLLDVL GAPKLRYLLH GMRRYLKNEH KEEFDIRLAS LQAS
