ID A0A1S3MF69_SALSA Unreviewed; 1208 AA.
AC A0A1S3MF69;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:0000313|RefSeq:XP_014001576.1};
GN Synonyms=RTEL1 {ECO:0000256|HAMAP-Rule:MF_03065};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014001576.1};
RN [1] {ECO:0000313|RefSeq:XP_014001576.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014001576.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {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_014001576.1; XM_014146101.1.
DR AlphaFoldDB; A0A1S3MF69; -.
DR STRING; 8030.ENSSSAP00000083080; -.
DR PaxDb; 8030-ENSSSAP00000083080; -.
DR Ensembl; ENSSSAT00000175669; ENSSSAP00000171014; ENSSSAG00000068081.
DR GeneID; 106572180; -.
DR KEGG; sasa:106572180; -.
DR CTD; 51750; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
DR Bgee; ENSSSAG00000068081; Expressed in ovary and 13 other cell types or tissues.
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; 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; 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; 1.
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:UP000087266}.
FT DOMAIN 7..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 853..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
SQ SEQUENCE 1208 AA; 134847 MW; 8D2B10B178FFEB0D CRC64;
MPPLTLKGIT VDFPFTPYEC QKDYMSKVIE CLQNKVNGVL ESPTGTGKTL CLLCATLAWR
DYFKDTISAR KIAEKMGGAE LFPNTQLASW GTAATDGDTT TYYTDIPKII YASRTHSQLT
QVINELKNTS YRPKVCVLGS REQLCINPEV MRQESNHLKV HMCRQKISTR SCVFYNNVEE
KSMDKDLVNS ILDVEDLVKA GIKQRVCPYY LSRSLKQQAE IIFMPYNYLL DPKSRRAHNI
ELKGAVVIFD EAHNVEKMCE ESTSFDLTPY DLASAIDAVD KLLAEQAKEA GRGDVSEDFN
MESINGGLKL DITTIAKIKQ ILLDLEAAID SYDVSDKGIT KPGSFIYELF QKAHLTFDTR
TPIFEALEQI TGYLAGKPGI FMNTNGLQKL ADIIQLVFCV DAQEGNKGAN MPPNMQSSTT
KFKVHIHKDT SHHKKKQNTD VWSSSSSKKQ GNVLSYWCFS PGISMQELVR QGVRSIILTS
GTLSPLSSFT SEMQIPFPVC LENSHVIQHD QIFVSIIDRG PDSVQLSSAF DRRFVPENMA
SLGNTVVNLG RIVPHGLLVF FPSYPVMDKT LEFWRANGHA DRIENIKPMF VEPRGKGTFT
EIIDGYYDKV NDSKSKGGSF FAVCRGKASE GLDFADTYGR GVIITGLPFP PRMDPRVILK
MQYLDEMCRK KTPGVQYLSG QNWYRQQASR AVNQAIGRVI RHRDDYGAIF LCDHRFKSTD
ARAQLPSWIR PYVRTYDNFG NVVRDVAQFF RVAQKLRPPP EKKPAKGSCG GVVHSADAQC
VSAGPCHSSE GSTKGGFAQK AKVLDSHVPS LKRRRLNEHG SSEGNGMARL CIEYETEMEA
SRRRPAGLLD ALEHSDSRYG DEDEALGGEE RANRISTLSL QYDKRVDDEL RGGKRKIKVV
QERKIPLSSD VSEEGKAGKA KSFLAEMKRS LSQVNFQRIM AALQTYKRMD DLDELLAEAA
DLFTGDANTH NLLRGFYQFI RPHHKKRFDE KCVELTGQGC DYKPDHSLSK EEKETLMQNG
AKPGKLTGVV VASDSSSSCS QLNASLLLNK GGHHLGIHRL TTEERLPKNQ VLTVDPKCED
QAPVQSAQKS QIYASFIAAV KKSIGLEKSN QLFSAIQSYK KTDNYDSLVG TVVSLLTEKN
EDFNLLSTFA LFIRPHHKKQ YREMLDALIG DSTGSSASSG ISGQLMQVST PGKAQRKISS
FFPSSQRK
//
