RTEL1_CULQU
ID RTEL1_CULQU Reviewed; 978 AA.
AC B0W9F4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=CPIJ003765;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS231864; EDS40179.1; -; Genomic_DNA.
DR RefSeq; XP_001845338.1; XM_001845286.1.
DR AlphaFoldDB; B0W9F4; -.
DR SMR; B0W9F4; -.
DR STRING; 7176.CPIJ003765-PA; -.
DR PRIDE; B0W9F4; -.
DR GeneID; 6035102; -.
DR KEGG; cqu:CpipJ_CPIJ003765; -.
DR VEuPathDB; VectorBase:CPIJ003765; -.
DR VEuPathDB; VectorBase:CQUJHB016693; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; B0W9F4; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; B0W9F4; -.
DR Proteomes; UP000002320; Partially assembled 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: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: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 Reference proteome.
FT CHAIN 1..978
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370619"
FT DOMAIN 7..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 265..268
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 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 222
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
SQ SEQUENCE 978 AA; 109437 MW; EC2F8A8860A2CE53 CRC64;
MPEYLINGIP VNFPFEPYQV QRDYMARVIE CLQNSSNGVL ESPTGTGKTL SLLCSSLAWI
LHKKAQVQAS QRTNVSELKE FEFEKKKMGG GGGGPKPEMD KLLDELNENS GKEGGRWGVP
KIIYASRTHS QLTQAMQEMK NTSYGFMRAV ILGSRDQLCI HPEVAKEEGN AVKTNLCKAK
IQARACSFYS RVEACKERPE ITGSTIMDIE DLVRVSTKLK ACPFFMSKEL IENADVLFMP
YNYLLDPKAR KANNLELANT IIILDEAHNV DKMCEESASM QIRSSDIALC IDDVTSIMKV
MDNTVAIPED DDAKKDFTID DLALLKEMLL SLEKTVDEIP VMFSQGGSTQ PGTYIFEIFE
KANIKEGNYH IIAQLLENII QYIATITEKN NFVRRGGGLQ ILAESLSIMF AGSGPQYRES
IDKCYKCHID IEEQKKVRGN TKQADGWTAT KQLVPSVKAN AKVINFWCFN PGFGMRQLLG
RNARSIILTS GTLAPLKPLI SELDIPIAVK LENPHIIDGS QVCVKIVGQG PDKESLNSSY
GNRDNPKYIS SLGRTILSFC PIIPGGLLVF FPSYPLLNKC QEAWQETGIW AQISRTKPIF
VEPRGKDQFL NTMTEYYAKI NDPDGKGAVF MAVCRGKVSE GLDFADMNGR ACIITGLPFP
PLKDARVILK KRYLQEVRTR ENEIISGDEW YSLEAARAVN QAIGRVIRHK NDYGAILLCD
NRFHNPRQKA QLSSWIQKHL NTAQHPTFGP IVRELSQFFR NAEKTLPQAK LTRSLAPLGP
EPPIALVPDS TSLLVSGETK KKLDDIKNNF IKIENSNAVT AFKLSDYQHA HRSDATAASG
KDFLSRLNTQ VRTIDFNDMS SAGPSSQAGL VAIHKRERSN ESTMVTQQKK RKVVLIPQET
ISLDDSLEVL EVKPERQAPE DRVELLKVIK SSIVPAQYKR FLVVLTGYRN DRDFGTMMGG
MVEIFNRPEL YYLLKGEI
