RTEL1_CAEBR
ID RTEL1_CAEBR Reviewed; 994 AA.
AC A8WS58;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=CBG02256;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601486; CAP23316.1; -; Genomic_DNA.
DR RefSeq; XP_002639805.1; XM_002639759.1.
DR AlphaFoldDB; A8WS58; -.
DR SMR; A8WS58; -.
DR STRING; 6238.CBG02256; -.
DR PRIDE; A8WS58; -.
DR EnsemblMetazoa; CBG02256.1; CBG02256.1; WBGene00025337.
DR GeneID; 8581799; -.
DR KEGG; cbr:CBG_02256; -.
DR CTD; 8581799; -.
DR WormBase; CBG02256; CBP14383; WBGene00025337; Cbr-rtel-1.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; A8WS58; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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; ISS: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_0000370615"
FT DOMAIN 15..324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 818..896
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; 112715 MW; A82E766EC047444C CRC64;
MVSNPSSSTE VWINSKTSIK FPFEPYECQR IFMKNVIDVL DMKLDAALES PTGTGKTLSL
LCSTLAWVQK LKESKPMDFA TWQSSGAGGA EKTEDKLKNS FIPTIFYASR THSQLEQVVH
ELNRTEYKWV KTTILGSREH FCINQKVKKI KESNRQAHVC RGLVSKRSCH YYNKFDALTT
DKANEILEKG EAMDIEDFVK IGTQNSICPY FMSRQRSETA ELILLPYNYI IDPKMRRRYK
LDLKNSIVIF DEAHNLESIC ESNASAELSS TSIALCIEEL KKVLALLVEE EENAREEADN
ETEAFGTQKI DLTKKLIENL RTEDLMALLE KVFTLEENFD KLFESDQLKS VPPLDGKASD
GAILLETLAN SGCDGNSVER FVDVLRDAIS YLLSKNEEVS LTEKGDGMES VADFLLSIYS
THAQEVAAAV GDEHIKLADR VDPATVARNC KLYIRKDSGK LVIKYFCFQA SISMRMLKMR
GVRNVLLASG TLSPIQAFTY NMGLNFGAIL ENEHALKQVP VLTSIVTRGK HGGLVGSFQN
RKNIEYVSDV GESLIRVMET TPQGVLVFFS SYSQMDELVE VWKKTKRGAS DSPETFWEKM
EKTKKIAVEP RAKEQLAAVR LRYTQGVSEP HGAALLAVCR GKVSEGIDFC DAESRAVIIV
GIPYPPIHDE RVVLKKMYLD DLMGRKDLTN EPQSSRDWYQ MEAFRAVNQA IGRVLRHKND
FGTVVLIDTR YASAKPEMFP KWLRNTISRC DSNNCALKTA RFFKERGHLI ENSKSEYIKK
QAKTCKSFRQ VKSQSASNPK DDITDITLED MFSPANMKIE KKEKIEPRPI KYDSSSSSVF
SLPTNEDELK VKKWEQENDS QTNVSSSSDL NKRKYKAETP GNSSGQHVVS GSEPPKKRKM
VLLTRETLPE KYQNALNIPT SELTKGMSLD NQKQFVATLK GYKATNMEWQ EVFQRLHQIF
IPDRPDLFIS CSNILRSEDK MKYIRRSLGM KINY
