ID A0A182MAW6_9DIPT Unreviewed; 1192 AA.
AC A0A182MAW6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Regulator of telomere elongation helicase 1 homolog {ECO:0000256|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03065};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA013798-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA013798-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA013798-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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:0000256|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:0000256|ARBA:ARBA00001665, ECO:0000256|HAMAP-
CC Rule:MF_03065};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|HAMAP-Rule:MF_03065}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03065}.
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DR EMBL; AXCM01000817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182MAW6; -.
DR STRING; 139723.A0A182MAW6; -.
DR EnsemblMetazoa; ACUA013798-RA; ACUA013798-PA; ACUA013798.
DR VEuPathDB; VectorBase:ACUA013798; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd13932; HN_RTEL1; 1.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 1.20.1160.20; -; 1.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
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; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 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}.
FT DOMAIN 7..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
SQ SEQUENCE 1192 AA; 135001 MW; 0009013A4EA5A483 CRC64;
MPEYIINGVP VNFPFEPYQL QKNYMAKVIE CLQNKSNGVL ESPTGTGKTL SLLCSSLAWL
LFMKSKVPQS CSDTLDTLHL PELSDLSPEE ALDRQEQEKD AKVKIIYASR THAQLSQAMQ
ELKNTGYHCV RAIVLGSRDQ LCIHGEISKQ DNNAIKTTLC REAVKSRRCS FYNRVEWVKD
RPAVTSVPVL DIEDLVKVGR KMKACPYYLS KELIEQADII FMPYNYLLDP KARKSNGLNL
QNSVIIVDEA HNVEKLCEEI GSAKLRSSDI ATAIEDTSTV IQVMMNAGEA VCSLDVDKQP
DFTVDDLVLL KEILLNVEKA VDGVSMMFSQ GGITHPGTYI FDLMEKANIK FGNVKAILKL
LNSLITHITT TMLNDFVRLG AGLQLVADFL EVVYAGNGPE YRQAIEKCFR VHIEFDESKQ
TTKGNVTRAN GWTASKQDIK ALAKPNSKVV NFWCFNPGFG MKRLLDSGPR SIILTSGTLA
PLKPLISELN MPVAVTLENP HIIGRNQVYV KVITHGPDRV ELNSSFKNRS NPKYLSSLGR
TALSLCPIIP GGLLIFFPSY PLLHKCCEEW QASGIWEQIN RIKTIFIEPR DKDSFLTTMA
EYYAKVRDPE SRGAIFMAVC RGKVSEGLDF VDANGRAVMI TGLPFPPMMD ARVMLKKEYL
DTNRTRENEL ITGNDWYSLE ASRAVNQAIG RVIRHKYDFG AILLCDSRFQ SARQQSQLST
WIHSHLRDER NAPKFGTVVG EMSSFFRNMA KFSAPARVRE VYTIELEDDE DENCCAEPAS
NTAADLPYDE KFRMNDYLYE SKQKHPLMDK NAQALNSSDP EASSSELVTL YKRELKNDHG
LLRSPKTCSD LNLVEHKHVL VPKKFIKIEP FESTIAHISV VEDSDVEIIE PGAEQQKPRI
AHNPLMQALD VEIIEPKVEP QETRIAHKPL KQASDVEIIE PMVEQREPRT SQENRVLVAR
KKRNQAYVPE KFIKIEPFES TSAAISVVED LDIEIIEPTA KQQEQHSAHK PLKQDSDVVI
IEPIAEQQES RTAHENRVLV ARKKALVSEK LIKIEPFEST SAHMPVVEDL KVEIIEPVVE
QNETRTAHKS LEEDSDVEII DPIAEQQEQR TAPESRVDFL HAIKSSLDVD KYKQFLRALS
VYHRDSNFTV FIERMVFCLE APHSLYLLRA MRRFVKPEHK LQFDIRMEQI TL
//
