RTEL1_AEDAE
ID RTEL1_AEDAE Reviewed; 1010 AA.
AC Q16X92;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=AAEL008960;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(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; CH477545; EAT39227.1; -; Genomic_DNA.
DR RefSeq; XP_001653621.1; XM_001653571.1.
DR AlphaFoldDB; Q16X92; -.
DR SMR; Q16X92; -.
DR STRING; 7159.AAEL008960-PA; -.
DR PRIDE; Q16X92; -.
DR GeneID; 5571306; -.
DR KEGG; aag:5571306; -.
DR VEuPathDB; VectorBase:AAEL008960; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; Q16X92; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q16X92; -.
DR Proteomes; UP000008820; 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: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; 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; 1.
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..1010
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370617"
FT DOMAIN 7..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 912..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 263..266
FT /note="DEAH box"
FT COMPBIAS 916..931
FT /note="Basic and acidic 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 157
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 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
SQ SEQUENCE 1010 AA; 113780 MW; 83277CCB759F0CA1 CRC64;
MPEYQINGIT VNFPFEPYQV QRDYMSRVIE CLQNSTNGVL ESPTGTGKTL SLLCSSLAWV
LHKKAQVQAN MRTNITDLKE FEMVQRKKLG GDGGSGMEEL LDKLHDGCGP EGAKWGVPKI
VYASRTHSQL TQVMQEMKNT SYSFMKGVIL GSRDQLCIHP EVSKEEGNST KTNLCKAKVQ
SRTCSFYSRV ESCKERPEVV SNVIMDIEDL VKVGTKVRAC PFFLSKELIE SADILFMPYN
YLLDPKARKA NNLEISNTII ILDEAHNVEK MCEESASMQI RSTDIALCID DVTSIMKVMD
HSVAIPEDDE TKKDFTIDDL ALLKEMLLQL EKTVDSIPVM FSQGGNTFPG TYIFEIFEKA
NIKEGNYHII AQLLENIIQY IATITEKNNF VRRGGGLQIL AEALSIIFAG SGPEYRASID
KCYKVHIEIE EQKKTRGNVK QADGWTATKQ LVPSVKANAK VVSFWCFNPG FGMRQLLGRN
ARSIILTSGT LAPLKPLISE LDIPIAVRLE NPHIIDGSQV CVKIVGQGPD KESLNSSYGN
RDNPKYISSL GRTILSFCPI IPGGLLVFFP SYPLLNKCQE AWQETGIWAQ ISRTKPIFVE
PRGKDQFLNT MSEYYQKIND PDGKGAVFMA VCRGKVSEGL DFADMNGRAV IITGLPFPPL
KDARVILKKK YLQEVRTREN EIISGDEWYS LEAARAVNQA IGRVIRHKND YGAILLCDNR
FHNHRQKSQL SSWIQKHLNT NQHQNFGPII GELSRFFRNA EKILPQSKLS RNIVTLVQEP
TPLIECNIPG ALIVNRDTKR KLDDIRNNFV QIENSNQVTS TFRISDYEQA PSQSASNEPK
NFLSRLNTQV HSIDFNDMTT YSMPSSSQGA LVGIHKRERS TGSDNSIFSQ TQTATQKKRK
VVLIPQQVIN LTSDDEDPGR TGDDPTRQAP EDRVELIKVI KTSIPLAKYQ AFLSTLTNYN
KDRNFDRLME GLLVAFDRPE LYYLLRAMRR FVKGDHEARF DAKIKEVCGR