RTEL1_DROVI
ID RTEL1_DROVI Reviewed; 1005 AA.
AC B4M891;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=GJ16649;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940653; EDW62367.1; -; Genomic_DNA.
DR RefSeq; XP_002056881.1; XM_002056845.2.
DR AlphaFoldDB; B4M891; -.
DR SMR; B4M891; -.
DR STRING; 7244.FBpp0231066; -.
DR EnsemblMetazoa; FBtr0232574; FBpp0231066; FBgn0203833.
DR GeneID; 6633257; -.
DR KEGG; dvi:6633257; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; B4M891; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; B4M891; -.
DR Proteomes; UP000008792; 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..1005
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370628"
FT DOMAIN 7..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 893..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 251..254
FT /note="DEAH box"
FT COMPBIAS 899..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 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOD_RES 876
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1005 AA; 111637 MW; 4FADD68C2F662574 CRC64;
MPENIIAGIP VHFPFEPYEV QRAYMEKVIM CLRDGTNGVL ESPTGTGKTL SLLCASLAWI
RTRQSEQQQY MQKLQLDQQK QATGGAGAGV ADLNAVMGKA NNWGVPKVIY ASRTHSQLSQ
AMRELKRTAY ANMKSVVLGS RDQLCIHPDV MREQGNSNKV NMCKLKVHAK TCSFQLRVES
KKDHPDFRGP SIMDIEDLVK VGQRLKMCPY FASKELVNGA DITFMPYNYL LDPKARKANK
IELSNTIVIL DEAHNIEKIC EESASVQIRS SDVAMAIEDI THIMKIFTSG DAQDTGGPEE
PKDFTLDDLT LLKEMLLELE KAIDGVVVDN KAEGTTYPAA HIYELLGKAN FTYGNCATIV
ALLDKLVQYL MVASQHSTML RKGGSFMVLA DLLNIVFANK EDVMSKVHRS FKVHVEIEDN
KQSKNAANSA KPQTGWLGKG NNAASSVTKA AKIINFWCFN PGFGMEQLLN AHVRSVILTS
GTLAPLKPLI AELAIPVAQH LENPHIVDRS QVYVKIIGTG PDREQLISNY KNRDNPKYIS
SLGQTILNVS RIVPDGLLVF FPSYPMLNQC VDAWQASGLW ADISCRKPIF LEPRGKDQFT
STMEEFYQAI RDSKGACFMA VCRGKVSEGL DFADRNGRAV IITGLPFPPL KDPKVVLKRR
YLETNRTKEN QLLSGQEWYN LDATRAVNQA IGRVIRHRND YGAILLCDAR FQDMSQVQQL
SKWIRGHLGA RPQSSPFGPI VRELRQFFKH AEQTMAQPEE RVVEPLLQTV CKEEQPTLAC
ASSSQITIKR EPGTGGTKFQ LASELAAQAE MANTIKTWTP ADYANAAGSS TLGRRAPDAM
DFMSRLNANV TSIDFNSADA GQDLVKIHKR ERSSPTASES SMIAKKRYKL IGNGPLKTEP
SEPATTSSSF CPTPAQSQLK EAPESRADFL REVRSVIDCD QFRSFGKALL AYKTGGDGCF
ETLMVLLLDV LGAPQLRYLL LGMRRYLKNE HKLEFDVRLA SFQAT
