RQL3_ARATH
ID RQL3_ARATH Reviewed; 713 AA.
AC Q9FT72; O81805; Q0WPC1; Q3E9Q7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ATP-dependent DNA helicase Q-like 3;
DE EC=3.6.4.12;
DE AltName: Full=RecQ-like protein 3;
DE Short=AtRecQ3;
DE Short=AtRecQl3;
GN Name=RECQL3; Synonyms=RECQ3, RQL3; OrderedLocusNames=At4g35740;
GN ORFNames=F8D20.250;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=11058127; DOI=10.1093/nar/28.21.4275;
RA Hartung F., Plchova H., Puchta H.;
RT "Molecular characterisation of RecQ homologues in Arabidopsis thaliana.";
RL Nucleic Acids Res. 28:4275-4282(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12856935; DOI=10.1023/a:1023968429220;
RA Bagherieh-Najjar M.B., de Vries O.M., Kroon J.T., Wright E.L.,
RA Elborough K.M., Hille J., Dijkwel P.P.;
RT "Arabidopsis RecQsim, a plant-specific member of the RecQ helicase family,
RT can suppress the MMS hypersensitivity of the yeast sgs1 mutant.";
RL Plant Mol. Biol. 52:273-284(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16371241; DOI=10.1016/j.jplph.2005.10.013;
RA Hartung F., Puchta H.;
RT "The RecQ gene family in plants.";
RL J. Plant Physiol. 163:287-296(2006).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LYS-64.
RX PubMed=19755539; DOI=10.1104/pp.109.144709;
RA Kobbe D., Blanck S., Focke M., Puchta H.;
RT "Biochemical characterization of AtRECQ3 reveals significant differences
RT relative to other RecQ helicases.";
RL Plant Physiol. 151:1658-1666(2009).
RN [8]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
CC -!- FUNCTION: 3'-5' DNA helicase that may play a role in the repair of DNA.
CC Exhibits an ATP or dATP-dependent DNA-helicase activity. Cannot use
CC GTP/dGTP, CTP/dCTP or UTP/dUTP as nucleotide cofactors. Catalyzes DNA
CC strand annealing. On nicked Holliday junctions, unwinds the lagging
CC strand. Cannot act on intact Holliday junctions.
CC {ECO:0000269|PubMed:19755539}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FT72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FT72-2; Sequence=VSP_039282;
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, young leaves,
CC shoots, shoot apical mersitem, inflorescences, flowers, siliques and
CC seeds. {ECO:0000269|PubMed:11058127, ECO:0000269|PubMed:12856935}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF01028.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA20044.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g35740 has been split into 2 genes: At4g35733 and At4g35740.; Evidence={ECO:0000305};
CC Sequence=CAB81483.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g35740 has been split into 2 genes: At4g35733 and At4g35740.; Evidence={ECO:0000305};
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DR EMBL; AJ404472; CAC14867.1; -; mRNA.
DR EMBL; AL031135; CAA20044.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161588; CAB81483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86556.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86557.1; -; Genomic_DNA.
DR EMBL; AK229155; BAF01028.1; ALT_INIT; mRNA.
DR PIR; T04679; T04679.
DR RefSeq; NP_195299.2; NM_119740.3. [Q9FT72-1]
DR RefSeq; NP_849500.1; NM_179169.1. [Q9FT72-2]
DR AlphaFoldDB; Q9FT72; -.
DR SMR; Q9FT72; -.
DR BioGRID; 15009; 1.
DR IntAct; Q9FT72; 1.
DR STRING; 3702.AT4G35740.1; -.
DR iPTMnet; Q9FT72; -.
DR PaxDb; Q9FT72; -.
DR PRIDE; Q9FT72; -.
DR ProteomicsDB; 226805; -. [Q9FT72-1]
DR EnsemblPlants; AT4G35740.1; AT4G35740.1; AT4G35740. [Q9FT72-1]
DR EnsemblPlants; AT4G35740.2; AT4G35740.2; AT4G35740. [Q9FT72-2]
DR GeneID; 829727; -.
DR Gramene; AT4G35740.1; AT4G35740.1; AT4G35740. [Q9FT72-1]
DR Gramene; AT4G35740.2; AT4G35740.2; AT4G35740. [Q9FT72-2]
DR KEGG; ath:AT4G35740; -.
DR Araport; AT4G35740; -.
DR TAIR; locus:2127998; AT4G35740.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_14_3_1; -.
DR InParanoid; Q9FT72; -.
DR OMA; TGKSFYY; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q9FT72; -.
DR PRO; PR:Q9FT72; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FT72; baseline and differential.
DR Genevisible; Q9FT72; AT.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..713
FT /note="ATP-dependent DNA helicase Q-like 3"
FT /id="PRO_0000394528"
FT DOMAIN 45..219
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 246..391
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 465..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 508..543
FT /evidence="ECO:0000255"
FT MOTIF 163..166
FT /note="DEAH box"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039282"
FT MUTAGEN 64
FT /note="K->M: Loss of ATPase or helicase activity."
FT /evidence="ECO:0000269|PubMed:19755539"
SQ SEQUENCE 713 AA; 79944 MW; 6AB1963C2C474EEC CRC64;
MKKSPLPVQN VQSSDKNVAG KEALVKLLRW HFGHADFRGK QLEAIQAVVS GRDCFCLMPT
GGGKSICYQI PALAKPGIVL VVSPLIALME NQVMALKEKG IAAEYLSSTQ ATHVKNKIHE
DLDSGKPSVR LLYVTPELIA TKGFMLKLRK LHSRGLLNLI AIDEAHCISS WGHDFRPSYR
QLSTLRDSLA DVPVLALTAT AAPKVQKDVI DSLNLRNPLV LKSSFNRPNI FYEVRYKDLL
DNAYTDLGNL LKSCGNICAI IYCLERTTCD DLSVHLSSIG ISSAAYHAGL NSKMRSTVLD
DWLSSKKQII VATVAFGMGI DKKDVRMVCH FNIPKSMESF YQESGRAGRD QLPSRSVLYY
GVDDRKKMEY LLRNSENKKS SSSKKPTSDF EQIVTYCEGS GCRRKKILES FGEEFPVQQC
KKTCDACKHP NQVAHCLEEL MTTASRRHNS SRIFITSSNN KTNEGQYSEF WNRNEDGSNS
NEEISDSDDA TEAANSVTGP KLSKKLGLDE KLVLLEQAEE KYYERNKQVK KSEKNAISEA
LRDSSKQRLL DALTRVLQLL ACVEEIDSQK GSEFLENECY RKYSKAGKSF YYSQIASTVR
WLGTASRDEL MTRLSSVVSL AREQEPLEEP LLATEPVENI EEEDDGKTNT VESRVDEPTQ
ELVVSPILSP IRLPQVPSFS EFVNRRKIKQ NTLIDKSSEG FDDKKPAKIM KLQ
