GenomeNet

Database: UniProt
Entry: M9PGH6_DROME
LinkDB: M9PGH6_DROME
Original site: M9PGH6_DROME 
ID   M9PGH6_DROME            Unreviewed;       985 AA.
AC   M9PGH6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 75.
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};
GN   Name=Rtel1 {ECO:0000313|FlyBase:FBgn0029798};
GN   Synonyms=Dmel\CG4078 {ECO:0000313|EMBL:AGB95108.1};
GN   ORFNames=CG4078 {ECO:0000313|EMBL:AGB95108.1,
GN   ECO:0000313|FlyBase:FBgn0029798}, Dmel_CG4078
GN   {ECO:0000313|EMBL:AGB95108.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA   An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95108.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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|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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014298; AGB95108.1; -; Genomic_DNA.
DR   RefSeq; NP_001259262.1; NM_001272333.1.
DR   RefSeq; NP_572254.1; NM_132026.2.
DR   AlphaFoldDB; M9PGH6; -.
DR   SMR; M9PGH6; -.
DR   EnsemblMetazoa; FBtr0070807; FBpp0070773; FBgn0029798.
DR   EnsemblMetazoa; FBtr0332398; FBpp0304672; FBgn0029798.
DR   GeneID; 31497; -.
DR   KEGG; dme:Dmel_CG4078; -.
DR   AGR; FB:FBgn0029798; -.
DR   CTD; 51750; -.
DR   FlyBase; FBgn0029798; Rtel1.
DR   VEuPathDB; VectorBase:FBgn0029798; -.
DR   HOGENOM; CLU_006515_4_0_1; -.
DR   OMA; GNCATIV; -.
DR   OrthoDB; 124793at2759; -.
DR   PhylomeDB; M9PGH6; -.
DR   BioGRID-ORCS; 31497; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 31497; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0029798; Expressed in gastric caecum (Drosophila) and 49 other cell types or tissues.
DR   ExpressionAtlas; M9PGH6; baseline and differential.
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; cd17970; DEAHc_FancJ; 1.
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; 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:UP000000803}.
FT   DOMAIN          7..303
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          863..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         146
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT   BINDING         164
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT   BINDING         173
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT   BINDING         209
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
SQ   SEQUENCE   985 AA;  109683 MW;  84CFDDC26EF255DC CRC64;
     MPESLIAGIP VHFPFEPYPV QRAYMEKVIH CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
     RTRQSEHQKQ MVKMEKADFS GLGGGAPGGD LSELAKTMGR ANNWGVPKVI YASRTHSQLT
     QAMRELKRTA YANMRSVVLG SRDQLCIHPE VMREQGNSNK TNMCKLRVHS KTCSFQMRVE
     SRKDHPDLRG PTIMDIEDLV KVGQRLKICP YFASRELVPQ ADITFMPYNY LLDPKARKAN
     KIELGNTIVI LDEAHNIEKI CEESASVQIK SSDVAMAIED VTHIMQVFAS GESQDMAGDE
     PKDFTLDDLT LLKEMLLELE KAIDAIVVDN AVDGTTFPAS MMYELLGKAN FTYGNVATIV
     SLLDKLVQYL LVASQQMSIR KGGTFTLLSD LLTIVFANKE DVMSKVYASF KVHVLVEESK
     QGHGKQQGAK QQGGWLGKGT IAAATGLSKV AKIINFWCFN PGFGMEQLLN TQVRSVILTS
     GTLAPLKPLI AELAIPVAQH LENPHIVDQS QVYVKIIGTG PDRQQLISNY ANRDNPKYIS
     SLGQTILNVA RIVPDGLLVF FPSYPMLNKC VDAWQASGLW ADISCKKPIF LEPRSKDQFT
     STMEEFYQAI RDSKGAVFMA VCRGKVSEGL DFADRNGRAV IITGLPFPPL KDPKVILKRR
     YLEANRTREN QLLSGQEWYN LDATRAVNQA IGRVIRHRND YGAILLCDSR FKDASQVQQL
     SKWIRGHLGD RPQCSPFGPI VRELRQFFKN AEANMKLPDE RETDSPLETV CKTEDEPLAA
     IPKVKREPGS NATFKSANES AIKVEMANSI KTWTPADYAS AAGHKLGGAA PNAMDFMSRL
     DSNVSSIDFN CCTDSKSGSS GLVKIHKRER SSPTAPESSS QVTKKRYKLV ENIKVEPSSS
     QAKEAPEERA AFLRELRSLV TQDQFRRFGK ALLEYKNGTY ESFQALMAIL LDVLSAPKVR
     YMLVGMRKYL KNEHKDEFDR RVGNL
//
DBGET integrated database retrieval system