ID A0A2Y9IP98_ENHLU Unreviewed; 1268 AA.
AC A0A2Y9IP98;
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=LOC111141622 {ECO:0000313|RefSeq:XP_022350036.1};
GN Synonyms=RTEL1 {ECO:0000256|HAMAP-Rule:MF_03065};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022350036.1};
RN [1] {ECO:0000313|RefSeq:XP_022350036.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022350036.1};
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_022350036.1; XM_022494328.1.
DR AlphaFoldDB; A0A2Y9IP98; -.
DR Proteomes; UP000248482; 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; 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; 1.
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:UP000248482}.
FT DOMAIN 7..295
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 980..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1182
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 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 206
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
SQ SEQUENCE 1268 AA; 138127 MW; D828423BD19A2AC2 CRC64;
MPKIALRGVT VDFPFQPYKC QEEYMSKVLE CLQKRVNGIL ESPTGTGKTL CLLCSALAWR
EHLRDAVSAR RIAERAPGEL FLDHTLSSWG AATSDGDTPA CYADIPKIVY ASRTHSQLTQ
AVGELRKTSY RPRVCVLGSR EQLCIHPEVK KQESSHMQIH LCRKKVASRS CHFYNNTEEK
SLEQELATTI LDIEDLVRSG NKHSLCPYYL SRSLKQRADI IFLPYNYLLD AKSRRAHSID
LKGTVVIFDE AHNVEKMCEE TASFDLTPHD LASGLDVLDQ VLEEQTKAAQ QGELHVEFST
AAHPGLHLEL QDLAKLKTIL LRLEGAIDAV ELPGNHSGVT KPGSYIFELF AEAQITLQTK
GCILDSLDQI IQHLAGRTGP FTSTAGLQKL SDIIQIVFTA DPAEGVPGSM VGPGVSQSYK
VHIHPDVGHQ RKAQRSDAWN TTAARKQGKV LSYWCFSPGH SMRELVRQGV RSVILTSGTL
APVSSLALEM QIPFPVCLEN PHVVSKQQIW VGIVPKGPDG AQLSSAFDRR FSDVCLSSLG
KALGNIARVV PHGLLVFFPS YPVMEKSLEF WRAHDFARKL ETLKPVFVEP RSKGGFSEVV
DAYYKQVAAP GSSGASFLAV CRGKASEGLD FADMNGRGVI VTGLPYPPRM DPRVVLKMQF
LDELKSLGGP GGQLLSGHEW YRQQASRAVN QAIGRVIRHR HDYGAIFLCD HRFTQPDARA
QLPSWVRPHV KVYDSFGHVI RDVAQFFRAA QKTTPVPAPL LAAPSLDEGQ GAVSAAMSPG
PLSTRKAKSL DVHVPSLRRR PTGSPATGDT ESSLCVEYER AQGLTQPRPV GLLAALERSE
QLAGGPADEA SPGEEEAQDL SAVCVPCTKR PAQEQRAGRR KIRVVGGHQE GPAAGAQTGR
ARLFMVAVKQ ALSPAGFHTF TRALQDYKGS DDLEALLACL SPLLAEDPEK HSLLQGFYQF
VRPHHKQRFE ELCLQRTGHG CSSQPELSLP QRPWAPAAQT PSGGKECDPK LTLARGAGQL
DPGQHLNQGR PHRVPRPAPA GDPSSRPKEG PRAPGAEKQG PPAVSAYLAD VRKALGSAGH
SQLLAALTTY KQDSDFEKVV AVVAALTTSR PEDLPLLQRF GMFLRPHHKQ RFRQTCADLM
GLAAPSAGTG VPGPQEASPS VPPNLAHSAS KPGAPQCEKR GTTPSKISAF LMPSRPPSAP
LRHAPSEWGS ACPGCGAEDT VPFQCPSCDF HRCQACWRQL LQASRTCPAC HAPARKQSIT
QVFWPEPQ
//
