RTEL1_DROWI
ID RTEL1_DROWI Reviewed; 998 AA.
AC B4NDG5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=GK24923;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH964239; EDW82871.1; -; Genomic_DNA.
DR RefSeq; XP_002071885.1; XM_002071849.1.
DR AlphaFoldDB; B4NDG5; -.
DR SMR; B4NDG5; -.
DR STRING; 7260.FBpp0254066; -.
DR PRIDE; B4NDG5; -.
DR EnsemblMetazoa; FBtr0255574; FBpp0254066; FBgn0226882.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; B4NDG5; -.
DR OMA; GNCATIV; -.
DR PhylomeDB; B4NDG5; -.
DR Proteomes; UP000007798; 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; IPR014001; Helicase_ATP-bd.
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; SM00487; DEXDc; 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..998
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370629"
FT DOMAIN 7..324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 426..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 254..257
FT /note="DEAH box"
FT COMPBIAS 430..454
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 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 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 998 AA; 111993 MW; 5D7871F1DF62A984 CRC64;
MPESIIAGIP VHFPFEPYEV QRAFMEKVII CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
RTRQSEQQKQ IRKLQDAANN TKVGPTGIVP GEAAELALTV GKANNWGVPK VIYASRTHSQ
LTQAMRELKR SAYAGMRSVV LGSRDQLCIH PEVMREQGNS NKVNMCKMRV HSKTCSFQLR
VESKKDHPDF RGPSIMDIED LVKVGQKLKM CPYFASKELV NDADITFMPY NYLLDPMARK
ANKIELSNTI VILDEAHNIE KICEESASVQ IKSSDVAVAI EDVTHIMRIF TSADSQDFSG
DEPKDFTLDD LTLLKEMLLE LEKAIDGVVV DNLAEGTTYP ASYMYELLAK ANFTYGNCAS
IVALLDKLVQ YLMVASQNNS SMIMRKGGSF LVLAELLTIV FANKEDIMAK VHRSFKVHVE
VEEAKQNAGK PAPKQQQQGG WLGKGNNTSN SSSSNKAKVI NFWCFNPGFG MEQLLNTQVR
SVILTSGTLA PLKPLIAELA IPVAQHLENP HIVDQSQVYV KIIGTGPDRQ QLISNFKNRD
NPKYISSLGQ TILNVSRIVP DGLLVFFPSY PMLNKCVDAW QTSGLWADIA AKKPIFLEPR
GKDQFTTTME EFYQAIRDSK GACFMAVCRG KVSEGLDFAD RNGRAVIITG LPYPPLKDPK
VILKRRYLEA NRTKENQLLT GQEWYNLDAT RAVNQAIGRV IRHRHDYGAI LLCDSRFQDN
SQVQQLSKWI RGHLGARPQC SPFGPIVREL RQFFRHAEET MEQPKERTDE PLLKNVYKTE
AVTQENNEEK PLFKVKREPG QMATNAAAFK QANEMAIKVE MTNSIKSWTP DDYVSAAGRT
QSHSQSKPPN AMDFMSRLDS NVSSIDFNST GTGNLVKIHK RERSSPTFGD TKSSSQLKKR
YKLVDNIKTE PSTSSSCKAP ESRADFLREV RCFINQDEFR DFGKALLAYK NGGDEAFESL
MSLLFKLLGK PQMRYLLLGI RRYLKNEHKA EFDKRVAT
