RQL1_ARATH
ID RQL1_ARATH Reviewed; 606 AA.
AC Q9FT74; Q9M9M2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP-dependent DNA helicase Q-like 1;
DE EC=3.6.4.12;
DE AltName: Full=RecQ-like protein 1;
DE Short=AtRecQ1;
DE Short=AtRecQl1;
GN Name=RECQL1; Synonyms=RECQ1, RQL1; OrderedLocusNames=At3g05740;
GN ORFNames=F10A16.2;
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], 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 TISSUE SPECIFICITY, AND INDUCTION BY ABIOTIC STRESSES.
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 [5]
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 [6]
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 {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Mostly expressed in shoots, flowers, siliques and
CC seeds, and, to a lower extent, in roots, seedlings, leaves, shoots,
CC shoot apical mersitem, and inflorescences.
CC {ECO:0000269|PubMed:11058127, ECO:0000269|PubMed:12856935}.
CC -!- INDUCTION: By cold. Repressed by drought.
CC {ECO:0000269|PubMed:12856935}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ404470; CAC14163.1; -; mRNA.
DR EMBL; AC012393; AAF26076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74288.1; -; Genomic_DNA.
DR RefSeq; NP_187225.2; NM_111448.3.
DR AlphaFoldDB; Q9FT74; -.
DR SMR; Q9FT74; -.
DR STRING; 3702.AT3G05740.1; -.
DR iPTMnet; Q9FT74; -.
DR PaxDb; Q9FT74; -.
DR PRIDE; Q9FT74; -.
DR ProteomicsDB; 226822; -.
DR EnsemblPlants; AT3G05740.1; AT3G05740.1; AT3G05740.
DR GeneID; 819743; -.
DR Gramene; AT3G05740.1; AT3G05740.1; AT3G05740.
DR KEGG; ath:AT3G05740; -.
DR Araport; AT3G05740; -.
DR TAIR; locus:2074429; AT3G05740.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_9_6_1; -.
DR InParanoid; Q9FT74; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q9FT74; -.
DR PRO; PR:Q9FT74; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FT74; baseline and differential.
DR Genevisible; Q9FT74; 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; IBA: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:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..606
FT /note="ATP-dependent DNA helicase Q-like 1"
FT /id="PRO_0000394527"
FT DOMAIN 215..391
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 413..563
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..338
FT /note="DEAH box"
FT COMPBIAS 153..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 606 AA; 68501 MW; A64E7FB793B0D324 CRC64;
MKDQDLELEK VRLISLATKL GFDEDSAKKC LDRFVDLYGD DGRDFITVEL CGDDFLAALA
DFEEGTEEWD DIQAIESEAQ GNLAEMFDKS TNPSDNGFDT DDDDDDSRVE VHVIEDSPEP
KKKPEIVELD SSSDLEDVET RFKVPRRSQT CSRSMDYSME DSVSTISGRK PSVQISNKDH
ETPSYEELQA LDDLEFANLV IFGNKVFRPL QHQACRASME RKDCFVLMPT GGGKSLCYQL
PATLKAGVTI VISPLLSLIQ DQIVALNLKF GIPATFLNSQ QTSSQAAAVL QELRRDNPSC
KLLYVTPEKI AGSSSFLETL RCLDRKGLLA GFVVDEAHCV SQWGHDFRPD YRELGCLKQN
FPRVPVMALT ATATESVCQD VLKSLRIPRA PVLKMSFDRI NLKYEVIVKT KEPLKQLQEL
LRDRFKDQSG IVYCLSKSEC VDVAKFLNEK CKVKTVYYHA GVPAKQRVDV QRKWQTGEVR
IVCATIAFGM GIDKADVRFV IHNTLSKAVE SYYQESGRAG RDGLQAQCIC LYQKKDFSRV
VCMLRNGQGR NMDRFKSAMA QAKKMQQYCE LKTECRRQML LEYFGESFDR MICKSSLNPC
DNCERS
