RTEL1_ANOGA
ID RTEL1_ANOGA Reviewed; 991 AA.
AC Q7QEI1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 5.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Regulator of telomere elongation helicase 1 homolog {ECO:0000255|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065};
GN ORFNames=AGAP000634;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_03065};
CC -!- SUBCELLULAR LOCATION: Nucleus {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; AAAB01008847; EAA06834.5; -; Genomic_DNA.
DR RefSeq; XP_311162.5; XM_311162.5.
DR AlphaFoldDB; Q7QEI1; -.
DR SMR; Q7QEI1; -.
DR STRING; 7165.AGAP000634-PA; -.
DR PaxDb; Q7QEI1; -.
DR GeneID; 1272449; -.
DR KEGG; aga:AgaP_AGAP000634; -.
DR CTD; 1272449; -.
DR VEuPathDB; VectorBase:AGAP000634; -.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; Q7QEI1; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q7QEI1; -.
DR Proteomes; UP000007062; Chromosome X.
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:0070182; F:DNA polymerase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
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:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0090657; P:telomeric loop disassembly; IBA:GO_Central.
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; 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; SSF52540; 1.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
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..991
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370618"
FT DOMAIN 7..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 812..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 254..257
FT /note="DEAH box"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
SQ SEQUENCE 991 AA; 110321 MW; 2639B1DDB0F5F6BD CRC64;
MPEYMINGIP VNFPFEPYEL QKNYMAKVIE CLQNKTNGVL ESPTGTGKTL SLLCSSMAWL
LHMKSKQPKH RMETIDTLPE PPELSNAKHA ALDPEQALAL QQQKANAKMK IIYASRTHSQ
LSQAMQELKN TSYLFVRSII LGSRDQLCIH PDISKQENNA IKTVLCRESV KARNCSFYNR
VETAKDRPDV ATVPVMDIED LVTVGRKLKA CPYYLSKELV EQADVIFMPY NYLLDPKARK
SNGLSLQNTV IILDEAHNVE KMCEEVGSAL LRSSDIALAI EDTSSVIKSM MDGGGAWTGD
GEKQLELTLD DLVLLKEILL GVEKAVDDIP ILFSQGGTTH PGTYIFDLLE KANIKFGNIN
VVLQVMNSLI THITTEKTGG FVRRGAGLQS MVDFLEVVFA SSGPEYRQAV EKCFRVHIEP
EEPKQLAKGG VKRADGWTAT KQPLKAPVKS TSKVINFWCF NPGFGMRQLV DSGTRSIILT
SGTLAPLKPF ISELSLPVAV SLENPHIIAR SQVYVKVITH GPDRVELNSS FKNRSNPEYI
ASLGRTALSL CPIIPGGLLI FFPSYPLLNK CSEEWQASGI WGQISRLKQI FVEPRGKDQF
TTTMAEYYAQ VRDPASRGAI FMAVCRGKVS EGLDFADANG RAVMITGLPF PPMMDARVVL
KKQYLDTNRT RENELITGND WYSLEASRAV NQAIGRVIRH KDDYGAILLC DSRFQNARQQ
AQLSAWIHSH LRESSAVPNF GTVVGEMSRF FRHMSTASLP ARVRDVCAVK DEPAEAAKEE
PGKGKRFATA VKGGGINTFA EKFRLSEYLP DSMKVNPHSR STKSAGDDAE AGGSGLVTLY
KRERNDGKGP PPSPGAFEAT RKRRKIVIVP QPLVKREDTE DGENVLLPVK QEPDVAAAAN
VKRVAPENRV DFLREVKCSL SAGSYKTFLQ SLAVYNRNSD FVLFIKQLCS CFNKPHLHYL
LLAMRRFIKQ EHTLEFDTII EKIEARFFSD M
