ID A0A2Y9QCB1_DELLE Unreviewed; 1344 AA.
AC A0A2Y9QCB1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Regulator of telomere elongation helicase 1 {ECO:0000256|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03065};
GN Name=RTEL1 {ECO:0000256|HAMAP-Rule:MF_03065,
GN ECO:0000313|RefSeq:XP_022453082.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022453082.1};
RN [1] {ECO:0000313|RefSeq:XP_022453082.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022453082.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03065};
CC -!- SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; the
CC interaction is direct and essential for suppressing telomere fragility.
CC Interacts with MMS19; the interaction mediates the association of RTEL1
CC with the cytosolic iron-sulfur protein assembly (CIA) complex.
CC {ECO:0000256|HAMAP-Rule:MF_03065}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03065}.
CC Note=Colocalizes with PCNA within the replication foci in S-phase
CC cells. {ECO:0000256|HAMAP-Rule:MF_03065}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03065}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03065}.
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DR RefSeq; XP_022453082.1; XM_022597374.2.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0000723; P:telomere maintenance; IEA:UniProtKB-UniRule.
DR CDD; cd17970; DEAHc_FancJ; 1.
DR CDD; cd13932; HN_RTEL1; 2.
DR CDD; cd16449; RING-HC; 1.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 1.20.1160.20; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_03065; RTEL1; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
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; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR030845; RTEL1.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 1.
DR Pfam; PF06733; DEAD_2; 2.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03065};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_03065};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03065};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03065};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03065};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 7..328
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 872..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 150..166
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT COMPBIAS 882..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 239
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
SQ SEQUENCE 1344 AA; 146804 MW; 6AFA96DA05A5479D CRC64;
MPKITLNGVT VDFPFQPYKC QEEYMSKVLE CLQKKVNGVL ESPTGTGKTL CLLCSTLAWR
EQLRDAVSAR KIAERVSGEL FLDRALASWG NAALEGDVPA CYADVPKIIY ASRTHSQLTQ
VISELRNTSY RPRVCVLGSR EQLCIHPEVK RQESNHTQVH LCRKKVASRS CHFYNNVEGA
ACCQEPFHPG CLPRSGYSGP ESLCLRPPVS PEKSLEPELA CRVLDIEDLV SSGTRHRVCP
YYLSRNLKQQ ADIIFMPYNY LLDAKSRRAY GIDLKGTVVV FDEAHNVEKM CEEAASFDLT
PHDVASGLDV IDQVLEEQAK VAWQAELHPE FSADSASSGL NLELEDLAKL KTILLRLEGA
IDAVELPGGD GGVTKPGSYI FELFAEAQIT FHTKGCILDS LDQIIQHLAG RAGLFTNTAG
LQKLADIIQI VFSVDPAEGG PSAMVGPGCQ SYKVHIHPDA GHRRTAQRSD AWNATAARKQ
GKVLSYWCFS PGHSMRELVH QGVRTLILTS GTLAPVSSFT LEMQIPFPVC LENPHVIDKH
QIWVGIVPKG PDGAQLSSAF DKRFSDECLS SLGKALGNIA RVVPHGLLVF FPSYPVMEKS
LEFWRAHDFA RKLEVLKPMF VEPRTKGGFS EVMEAFYTRV AAPGSSGATF LAVCRGKASE
GLDFADANGR GVIVTGLPYP PRMDPRVVLK MQFLDEMKGQ NGARDQFLSG HDWYRQQASR
AVNQAIGRVI RHRHDYGAVF LCDHRFSSAD ARAQLPSWVR PHVKVYDSFG HVIRDVAQFF
RIAQRTMPVL APRAAAPSLG EGEGTASVAV SPGLLRTRKA TSLDVHVPSL RRRRTGLLVA
GDAEGSLCVE YQQEAVQARR RPVGLLAALE HSEQLAEGPG DKALPAEEEA PRHSAPWGPR
EKRPAEEQRG RRRKVRLVGG PEGPEAGADT GRAKLFMAAV KQALSQASFD TFTRALREYK
STDDLAALAA HLGPLFAEDP KKHSLLQGFY QFVRPHHKQQ FEEVCRQLTG RGCSFRPEYG
LPRRQGAQPA LDPSGEAGPA RVGPSNSDPE DPSPPWSCSG PSGTSWAPPR LRVSSGRREP
DPKLTVSQGA ARQLDPREHL NQGRPHLASG LLPAGDPSRR PPEGSGAPGA KKHPPAVSAY
LADAHRALGA TGYSQLLAAL TTYKQDDDLE KVVAVVASLT TARPEDLTLL QRFGMFVRPH
HKQRFQQTCV DLGTQAPGPW EGSPAAPSDL VCGARGPGPS LPEKPPGKTQ SKISSFLTQR
PARGAGAPGR PPGAPCGQAQ SEWVGLVCPG CRAEDVVPFQ CPSCDFHCCR ACWRQHLQVS
RTCPACHAAT RKQSLTQVFW PEPQ
//
