RTEL1_DANRE
ID RTEL1_DANRE Reviewed; 1177 AA.
AC P0C928;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Regulator of telomere elongation helicase 1 {ECO:0000255|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065};
GN Name=rtel1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: ATP-dependent DNA helicase implicated in telomere-length
CC regulation, DNA repair and the maintenance of genomic stability. Acts
CC as an anti-recombinase to counteract toxic recombination and limit
CC crossover during meiosis. Regulates meiotic recombination and crossover
CC homeostasis by physically dissociating strand invasion events and
CC thereby promotes noncrossover repair by meiotic synthesis dependent
CC strand annealing (SDSA) as well as disassembly of D loop recombination
CC intermediates. Also disassembles T loops and prevents telomere
CC fragility by counteracting telomeric G4-DNA structures, which together
CC ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP-
CC 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; BX004876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009304167.1; XM_009305892.2.
DR AlphaFoldDB; P0C928; -.
DR SMR; P0C928; -.
DR STRING; 7955.ENSDARP00000105420; -.
DR PaxDb; P0C928; -.
DR GeneID; 503732; -.
DR CTD; 51750; -.
DR ZFIN; ZDB-GENE-050306-11; rtel1.
DR eggNOG; KOG1132; Eukaryota.
DR InParanoid; P0C928; -.
DR OrthoDB; 186062at2759; -.
DR PRO; PR:P0C928; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
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:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0090657; P:telomeric loop disassembly; IBA:GO_Central.
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; PS00690; DEAH_ATP_HELICASE; 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..1177
FT /note="Regulator of telomere elongation helicase 1"
FT /id="PRO_0000370614"
FT DOMAIN 7..302
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 847..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 151..167
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 250..253
FT /note="DEAH box"
FT MOTIF 883..889
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
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 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
SQ SEQUENCE 1177 AA; 132804 MW; CA613CA7DD45A138 CRC64;
MPVIKLKGIN VDFPFTPYPC QEDYMSKVIE CLQKKVNGVL ESPTGTGKTL CLLCSTLAWR
DHFKDTISAR KITERMGGAE LFADRPMSSW GTAATDGDTP TYYTDIPKII YASRTHSQLT
QVVNELKNTS YRPKICVLGS REQLCINQEV MRHESNHIKV HMCRAKVSSR SCIFYNNVDE
KSTDKEIVNS ILDVEDLVKT GKKQRVCPYY LSRSLKQHAD VIFMPYNYLL DPKSRRAHNI
ELKGAVVIFD EAHNVEKMCE ESTSFDLTPH DLISAIEAVD RLLREQASDI SKADSAEDFN
VESLNSGLKM DITTIAKVKQ ILMDLETAIN DFEMPANNQG ITKPGSFIFE LFEMANVNSK
TKTETVEAME QITGYLAGRP GVFLNTSGLQ KVADIIQLVF VAEPAEGSKK SQTGNSLKEF
KVHIHPDNSN FKKKQITDVW ASSSTKKQGN VLSYWCFSPG FSMQELLRQE VRCIILTSGT
LSPLSSFTCE MQIPFPVSLE NPHVIQRDQI FVSIIEKGPD GVQLSTAFDR RFVPENMSSM
GNTLVNLSRV VPHGLLVFFP SYPVMDKTLE FWRAKGHADR IENVKPMFVE PRGKGTFTEV
IDGYYGKVDD PNSSGGSFFA VCRGKASEGL DFADTYGRGV VITGLPFPPR MDPRVVLKMQ
YLDEMCRNKI SGVKYLTGQE WYRQQASRAV NQAIGRVIRH REDYGAIFLC DHRFKSADAR
NQLPSWVRPY VKIYDGFGTM VRDVAQFFRT AQKTRPVPVK KGKAEGHENQ ADTRLLNTGS
SCLTKSVWPS DIYQKAKTLD AHVPSLKRRK LDSEEHSGRE GAARLCIQYE MEMTSKRKPV
SLLDALDDTT DKEEREDTMV GEERASHLST LSLQHDKRLD DESRGGKRKI KVVQERETVT
SHTAKTGKAF MMELRRCLSH ENFKLIMEAL QSYKTADNLN NLLATVAEPL IQDHNTHSLL
RGLYQFIRPH HKKEYDERCL ELTGEGCGYK QEHSLSREEK EALRHNSVKA EIPPVNPPIE
QLNSSRLLNQ GGSHLGTIQL NGGEVNVRSE EQKPQTSIKE GPSCSSLLSD IKQAIGAEKT
RQMFSALQAY KTSNNYEQMV STVVSLLTER DEDIALLERL SVLIRPQHRK QFGELLKSLT
GNDSAVVQDS DIGSSQQLSY LEERLNARYR PSFHECC
