ID   RTEL1_CAEEL             Reviewed;         994 AA.
AC   Q93575; P90854; P90855;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 3.
DT   03-AUG-2022, entry version 141.
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   Name=rtel-1 {ECO:0000255|HAMAP-Rule:MF_03065};
GN   Synonyms=bch-1 {ECO:0000255|HAMAP-Rule:MF_03065}; ORFNames=F25H2.13;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18957201; DOI=10.1016/j.cell.2008.08.016;
RA   Barber L.J., Youds J.L., Ward J.D., McIlwraith M.J., O'Neil N.J.,
RA   Petalcorin M.I.R., Martin J.S., Collis S.J., Cantor S.B., Auclair M.,
RA   Tissenbaum H., West S.C., Rose A.M., Boulton S.J.;
RT   "RTEL1 maintains genomic stability by suppressing homologous
RT   recombination.";
RL   Cell 135:261-271(2008).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20203049; DOI=10.1126/science.1183112;
RA   Youds J.L., Mets D.G., McIlwraith M.J., Martin J.S., Ward J.D., Oneil N.J.,
RA   Rose A.M., West S.C., Meyer B.J., Boulton S.J.;
RT   "RTEL-1 enforces meiotic crossover interference and homeostasis.";
RL   Science 327:1254-1258(2010).
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, ECO:0000269|PubMed:18957201,
CC       ECO:0000269|PubMed:20203049}.
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   -!- DISRUPTION PHENOTYPE: Viable, although the brood size is reduced and
CC       the life cycle is retarded (at 20 degrees Celsius, worms take 24 hours
CC       longer to reach the gravid adult stage). The smaller brood size may
CC       result from replicative stress, which is often associated with a
CC       persistence of unrepaired DNA damage during development. Mutants show
CC       defective crossover interference with all double-strand breaks becoming
CC       crossovers and a compromised homeostasis after ionizing radiation.
CC       Synthetic lethality in worms lacking both rtel-1 and him-6, with a
CC       marked increase in the number of foci representing unresolved
CC       recombination intermediates. {ECO:0000269|PubMed:18957201,
CC       ECO:0000269|PubMed:20203049}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03065}.
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DR   EMBL; Z79754; CAB02102.1; -; Genomic_DNA.
DR   EMBL; Z83224; CAB02102.1; JOINED; Genomic_DNA.
DR   PIR; T21356; T21356.
DR   RefSeq; NP_492769.1; NM_060368.4.
DR   AlphaFoldDB; Q93575; -.
DR   SMR; Q93575; -.
DR   BioGRID; 38360; 2.
DR   IntAct; Q93575; 2.
DR   MINT; Q93575; -.
DR   STRING; 6239.F25H2.13.2; -.
DR   EPD; Q93575; -.
DR   PaxDb; Q93575; -.
DR   PRIDE; Q93575; -.
DR   EnsemblMetazoa; F25H2.13.1; F25H2.13.1; WBGene00009124.
DR   EnsemblMetazoa; F25H2.13.2; F25H2.13.2; WBGene00009124.
DR   GeneID; 172946; -.
DR   KEGG; cel:CELE_F25H2.13; -.
DR   UCSC; F25H2.13; c. elegans.
DR   CTD; 172946; -.
DR   WormBase; F25H2.13; CE15894; WBGene00009124; rtel-1.
DR   eggNOG; KOG1132; Eukaryota.
DR   GeneTree; ENSGT00950000182970; -.
DR   HOGENOM; CLU_006515_4_0_1; -.
DR   InParanoid; Q93575; -.
DR   OMA; GNCATIV; -.
DR   OrthoDB; 186062at2759; -.
DR   PhylomeDB; Q93575; -.
DR   PRO; PR:Q93575; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00009124; Expressed in germ line (C elegans) and 4 other tissues.
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: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; IGI:UniProtKB.
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; 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; 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..994
FT                   /note="Regulator of telomere elongation helicase 1 homolog"
FT                   /id="PRO_0000370616"
FT   DOMAIN          15..300
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   REGION          876..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           251..254
FT                   /note="DEAH box"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         142
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         169
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"
SQ   SEQUENCE   994 AA;  112945 MW;  244F62A5E973B7C2 CRC64;
     MPPKASNSTE VWINPKLSVK FPFEPYECQR IFMKNVVDVL DRKLDAALES PTGTGKTLSL
     LCSTLAWVQR QKETKPLDFA TWQTSGAGGA EKTDEKLKSA YVPTIFYASR THSQLEQVVH
     ELNRTEYKWV KTTILGSREH FCINQKVKKI KESNRQAHVC RGLVSKRACH YYNKFDACTT
     DKMTEFLDKG EAMDIEDFVK LGTQNSLCPY FMSRQRSETA ELILLPYNYI IDPKMRRRYK
     LDLKNSIVIF DEAHNLESIC ESNASAELTS TSIALCIEEL KKVLALLVDE EETARSEADA
     ETGAFGSAKI DLTKKLIENL RTEDLMTVLE KIFSLEEEMD KLFGSSQLKS VPPLSGKASD
     GEILLETLAK AGFDANSVER LVDVLRDAIS YLLSKNEEVA LTEKGDGMEK VADFLLSIYS
     THAQDVAAAV GEETVKLVDR VDPKTVARNC KLYIQKDKDN EKLTIKYFCF QASISMRMLK
     MRGVRNVLLA SGTLSPIQAF TYNMGLNFGA ILENEHALKQ VPVLTSIVTR GKRGGLAGSF
     QNRKNLDYVT GVAEALLRVM EVIPQGILIF FSSYSQMDEL VATWKTTKWS SNSNESFWEK
     MEKTKRVVVE PRAKEELAAI RLRYTQGVSE QHGAALLAVC RGKVSEGIDF CDAESRAVII
     IGIPYPPIHD ERVVLKKMYL DDLMGRKDTK SERQSSQDWY QMEAFRAVNQ AIGRVLRHKD
     DFGTVVLMDT RYASAKPEMF PKWLRNTISR SDTDGCALKT SRFFKERGHL IENSKTEYIK
     KQAKQCKSFR QVKQTAASDS KDDIIEITLE DMFSPANMKL EKKEITKLRP PQLIPSTSSV
     FSLPTNEDEL KIKKWEQEND IQCLSSIPLE SNKRKFKIET PGPSTSTLTQ KSEPPKKKKI
     LLLTRNTLPD EYQKAIEIPT SELLKDMSDD NKKQFATTLR SYKAESIRWD EVFQRFRPIF
     VPHKADLFIA CSNVLRSEDK MKYLKKALES KIHT