RTEL1_PONAB
ID RTEL1_PONAB Reviewed; 1302 AA.
AC Q5RE34;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 {ECO:0000255|HAMAP-Rule:MF_03065};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:0000255|HAMAP-Rule:MF_03065}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}.
CC Note=Colocalizes with PCNA within the replication foci in S-phase
CC cells. {ECO:0000255|HAMAP-Rule:MF_03065}.
CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the
CC interaction with PCNA and localization to replication foci.
CC {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; CR857704; CAH89973.1; -; mRNA.
DR RefSeq; NP_001124929.1; NM_001131457.1.
DR AlphaFoldDB; Q5RE34; -.
DR SMR; Q5RE34; -.
DR GeneID; 100171800; -.
DR KEGG; pon:100171800; -.
DR CTD; 51750; -.
DR eggNOG; KOG1132; Eukaryota.
DR InParanoid; Q5RE34; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000001595; Unplaced.
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: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; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
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; 2.
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; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 2: Evidence at transcript level;
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..1302
FT /note="Regulator of telomere elongation helicase 1"
FT /id="PRO_0000370612"
FT DOMAIN 7..297
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 758..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..168
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 251..254
FT /note="DEAH box"
FT MOTIF 873..879
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 1180..1187
FT /note="PIP-box"
FT COMPBIAS 1173..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 173
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 1302 AA; 142673 MW; 05591DABC80FAE4A CRC64;
MPKIVLNGVT VDFPFQPYKC QQEYMTKVLE CLQQKVNGIL ESHTGTGKTL CLLCTTLAWR
EHLRDGISAR KIAERVQGEL FPDRALSSWG NAAAAAAGDP IACYTDIPKI IYASRTHSQL
TQVINELRNT SYRPKVCVLG SREQLCIHPE VKKQESNHIQ IHLCRKKVAS RSCHFYNNVE
EKSLEQELAS PILDIEDLVK SGSKHRVCPY YLSRNLKQQA DIIFMPYNYL LDAKSRRAHN
IDLKGTVVIF DEAHNVEKMC EESASFDLTP HDLASGLDII DQVLEEQTKT AQQGEPHPEF
SADSTSPGLN MELEDIAKLK MILLRLEGAI DAVELPGDDS GVTKPGSYIF ELFAEAQITF
QTKVCILDSL DQIIQHLAGR AGVFTNTAGL QKLADIIQIV FSVDPSEGGP GSLAGLGALQ
SYKVHIHPDA GHRQTAQRSD AWSTTAARKR GKVLSYWCFS PGLSMRELVR QGVRSLILTS
GTLAPVSSFA LEMQIPFPVC LENPHIIDKH QIWVGVVPRG PDGAQLSSAF DRRFSEECLS
SLGKALGNTA RVVPCGLLIF FPSYPVMEKS LEFWRARDLA RKMEALKPLF VEPRSKGSFS
ETISAYYARV AAPGSTGATF LAVCRGKASE GLDFSDTNGR GVIVTGLPYP PRMDPRVVLK
MQFLDEMKGQ GGAGGQFLSG QEWYRQQASR AVNQAIGRVI RHRQDYGAVF LCDHRFAFAD
ARAQLPSWVR PHVRVYDNFG HVIRDVAQFF RVAERTMPAP APRATAPSVR EGEDAVREVK
SPGPLFSTRK AKSLDLHVPS LKQRSSGSAA AGDPESSLCV EYEQEPIPAR QRPRGLLAAL
EHSEQQAGSP GEEQAHSCST LFLLSAKRPA EEPRGGRKKI RLVSHPEEPV AGAQTDRAKL
YMVAVKQELS QANFATFTQA LQDYKGSDDF AALAACLGPL FAEDPKKHSL LQGFYQFVRP
HHKQQFEEVC IQLTGRGCGY RPEHSIPRRQ PAQPVLDPTG RTAPDPKLTL SKAAAQQLDP
REHLNQGRPH LSPRPPPTGD PGSHPQWRSG VPRAGKQGQR AVSAYLADAR RALGSAGCSQ
LLAALRAYKQ DDDLDKVLAV LAALTTAKPE DFPLLHRFSM FVRPHHKQRF SQTCTDLTGR
PYPGMERPGP QEESLVVPPV LTHGAPQPGP SRSEKPGKTQ SKISSLLRQR PAGTVGAGSE
DAGPSQSPGP PHGPAASEWG EPHGRDIAGQ QAAGAPGGPL SAGCVCQGCG AEDVVPFQCP
ACDFQRCQAC WQRHLQASRM CPACHTASRK QSVTQVFWPE PQ
