RQL5_ARATH
ID RQL5_ARATH Reviewed; 911 AA.
AC Q0WVW7; Q8W028; Q9C6N0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent DNA helicase Q-like 5;
DE EC=3.6.4.12;
DE AltName: Full=RecQ-like protein 5;
DE Short=AtRecQ5;
DE Short=AtRecQl5;
GN Name=RECQL5; Synonyms=RECQ5, RQL5; OrderedLocusNames=At1g27880;
GN ORFNames=F28L5.4;
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].
RC STRAIN=cv. Columbia;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, 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 [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 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, seedlings, shoots, shoot
CC apical mersitem, flowers, and siliques. {ECO:0000269|PubMed:12856935}.
CC -!- INDUCTION: Repressed by drought. {ECO:0000269|PubMed:12856935}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50580.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD13472.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ421618; CAD13472.1; ALT_INIT; mRNA.
DR EMBL; AC079280; AAG50580.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30887.1; -; Genomic_DNA.
DR EMBL; AK226619; BAE98731.1; -; mRNA.
DR RefSeq; NP_174109.2; NM_102553.5.
DR AlphaFoldDB; Q0WVW7; -.
DR SMR; Q0WVW7; -.
DR STRING; 3702.AT1G27880.1; -.
DR iPTMnet; Q0WVW7; -.
DR PaxDb; Q0WVW7; -.
DR PRIDE; Q0WVW7; -.
DR ProteomicsDB; 226543; -.
DR EnsemblPlants; AT1G27880.1; AT1G27880.1; AT1G27880.
DR GeneID; 839681; -.
DR Gramene; AT1G27880.1; AT1G27880.1; AT1G27880.
DR KEGG; ath:AT1G27880; -.
DR Araport; AT1G27880; -.
DR TAIR; locus:2029799; AT1G27880.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_10_2_1; -.
DR InParanoid; Q0WVW7; -.
DR OMA; AYCYTIV; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q0WVW7; -.
DR PRO; PR:Q0WVW7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WVW7; baseline and differential.
DR Genevisible; Q0WVW7; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..911
FT /note="ATP-dependent DNA helicase Q-like 5"
FT /id="PRO_0000394531"
FT DOMAIN 278..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 470..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..393
FT /note="DEAH box"
FT COMPBIAS 52..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 14
FT /note="A -> E (in Ref. 1; CAD13472)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="S -> L (in Ref. 4; BAE98731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 100755 MW; C4E0E98BAB3DF866 CRC64;
MDFDSDSDGS HVSATPPRDS FPSSPPQLQS PAKHVPPVSR KMTSSSSRSK PKAPTHPPPN
PSQEAPVPSP YPPPPPPSPL FTNLPFRICQ SQPARFSSSV SSFSRLCSRA SFTSVEKLKS
DGVDFVPEPP LVEVIAPPKS VRRKPPNLIT DTITSPPVKP MVFRSNGNGE GNFVKLNLNG
KRGKKFPSKY KGVSKSRSSY SFRGKRYKKK EADGDGESLL EEESDLQKQI EDEANGFISS
VEDAILAVKT EASDENLTKL LNLVYGYDSF RDGQLQAIKM ILGGSSTMLV LPTGAGKSLC
YQIPAMILPG ITLVVSPLVS LMIDQLKHLP SIIKGGLLSS SQRPEEATET LRKLKEGIIK
VLFVSPERLL NVEFLSMFRM SLSVSLVVVD EAHCVSEWSH NFRPSYMRLK ASMLFSELKA
ECILAMTATA TTMTLQAVMS SLEIPSTNLI QKSQLRDNFE LSVSLSGANR MKDLLILMES
PPYKEIRSII VYCKFQYETD MISKYLRDNN INAKGYHSGL PAKDRVRIQE SFCSNKIRVV
VATVAFGMGL DKGDVGAVIH FSVPGSMEEY VQEIGRAGRD GRLSYCHLFY DNDTYLKLRS
LAHSDGVDEY AVGKFLTHVF STETKQHEKI CSLVIESASQ KFDMKEEVMQ TILTHLELGE
VQYLRMLPQL NICCTLNFHK SSPNTLAARS AIVAAILKKS HVKQGLHVFD IPAVASSICV
ATTDVLAEIQ ALKMKGEVTY ELKDSAFCYT ILKSPKEICS LSSHLTKWLT EIESCKVRKL
DIMSSAAVAA ISVSNTSELS SGAKQTRSLQ SRIFDYFNGD EKCDSPSKAT QNCAFLRADI
KVFLQSNRQA KFTPRAIARI MHGVGSPAFP NSVWSKTHFW GRYMNVDFRV IMEAAQTELF
NFVDRNAALA T
