RQL4A_ARATH
ID RQL4A_ARATH Reviewed; 1188 AA.
AC Q8L840; O04092; Q9FT71;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP-dependent DNA helicase Q-like 4A;
DE EC=3.6.4.12;
DE AltName: Full=RecQ-like protein 4A;
DE Short=AtRecQ4A;
DE Short=AtRecQl4A;
DE AltName: Full=SGS1-like protein;
DE Short=AtSGS1;
GN Name=RECQL4A; Synonyms=RECQ4A, RQL4A, SGS1; OrderedLocusNames=At1g10930;
GN ORFNames=T19D16.15;
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=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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16146519; DOI=10.1111/j.1365-313x.2005.02501.x;
RA Bagherieh-Najjar M.B., de Vries O.M., Hille J., Dijkwel P.P.;
RT "Arabidopsis RecQI4A suppresses homologous recombination and modulates DNA
RT damage responses.";
RL Plant J. 43:789-798(2005).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18000056; DOI=10.1073/pnas.0705998104;
RA Hartung F., Suer S., Puchta H.;
RT "Two closely related RecQ helicases have antagonistic roles in homologous
RT recombination and DNA repair in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18836-18841(2007).
RN [9]
RP FUNCTION.
RX PubMed=19096507; DOI=10.1371/journal.pgen.1000285;
RA Hartung F., Suer S., Knoll A., Wurz-Wildersinn R., Puchta H.;
RT "Topoisomerase 3alpha and RMI1 suppress somatic crossovers and are
RT essential for resolution of meiotic recombination intermediates in
RT Arabidopsis thaliana.";
RL PLoS Genet. 4:E1000285-E1000285(2008).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21265901; DOI=10.1111/j.1365-313x.2010.04438.x;
RA Higgins J.D., Ferdous M., Osman K., Franklin F.C.;
RT "The RecQ helicase AtRECQ4A is required to remove inter-chromosomal
RT telomeric connections that arise during meiotic recombination in
RT Arabidopsis.";
RL Plant J. 65:492-502(2011).
RN [11]
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 involved in DNA repair (PubMed:16146519,
CC PubMed:18000056, PubMed:19096507). Required for the maintenance of
CC genome stability by modulation of the DNA damage response and
CC repression of crossovers. Confers resistance to genotoxic stress
CC (PubMed:16146519, PubMed:18000056). Suppresses spontaneous homologous
CC recombination (HR) events in somatic cells together with its partners
CC RMI1 and TOP3A (PubMed:19096507). Contributes to the maintenance of
CC chromosome integrity during meiosis. Involved in the removal of
CC telomeric bridges that appear to arise during meiotic recombination.
CC Required to resolve or dissolve MSH4-dependent telomeric associations.
CC Does not seem required for chiasma formation (PubMed:21265901).
CC {ECO:0000269|PubMed:16146519, ECO:0000269|PubMed:18000056,
CC ECO:0000269|PubMed:19096507, ECO:0000269|PubMed:21265901}.
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:0000269|PubMed:21265901}. Chromosome
CC {ECO:0000269|PubMed:21265901}. Note=Associates with recombination
CC intermediates and telomeres of meiotic chromosomes.
CC {ECO:0000269|PubMed:21265901}.
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 -!- INDUCTION: By cold. Repressed by abscisic acid (ABA).
CC {ECO:0000269|PubMed:12856935}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to genotoxic stress such as
CC UV light, methyl methanesulfonate (MMS) and mitomycin C (MMC), and
CC hyperrecombination (HR) during cell division.
CC {ECO:0000269|PubMed:16146519, ECO:0000269|PubMed:18000056}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC14868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ404473; CAC14868.1; ALT_INIT; mRNA.
DR EMBL; U95973; AAB65484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28665.1; -; Genomic_DNA.
DR EMBL; AY120761; AAM53319.1; -; mRNA.
DR EMBL; BT010133; AAQ22602.1; -; mRNA.
DR PIR; B86243; B86243.
DR RefSeq; NP_172562.2; NM_100968.3.
DR AlphaFoldDB; Q8L840; -.
DR SMR; Q8L840; -.
DR STRING; 3702.AT1G10930.1; -.
DR PaxDb; Q8L840; -.
DR PRIDE; Q8L840; -.
DR ProteomicsDB; 226906; -.
DR EnsemblPlants; AT1G10930.1; AT1G10930.1; AT1G10930.
DR GeneID; 837636; -.
DR Gramene; AT1G10930.1; AT1G10930.1; AT1G10930.
DR KEGG; ath:AT1G10930; -.
DR Araport; AT1G10930; -.
DR TAIR; locus:2197394; AT1G10930.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_0_1_1; -.
DR InParanoid; Q8L840; -.
DR OMA; SEYCKYK; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q8L840; -.
DR BRENDA; 3.6.4.12; 399.
DR PRO; PR:Q8L840; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L840; baseline and differential.
DR Genevisible; Q8L840; 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:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
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:0071215; P:cellular response to abscisic acid stimulus; IEP:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0051276; P:chromosome organization; IMP:TAIR.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
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; IMP:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
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; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromosome; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1188
FT /note="ATP-dependent DNA helicase Q-like 4A"
FT /id="PRO_0000394529"
FT DOMAIN 462..637
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 662..807
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1018..1100
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 311..346
FT /evidence="ECO:0000255"
FT MOTIF 581..584
FT /note="DEAH box"
FT COMPBIAS 993..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 475..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1188 AA; 133312 MW; 5D228599ADA134E4 CRC64;
MINSNQMSRS HLPEVQKPRG PQTNWSEHAK ALESSSSVTK FLSSNVLYAL ESQKPRDMAA
RSIAFPSVNV HTLAHPQISK AWRALSSLSV NNTYLRPGVT PPIDVGTNDS YSARERSTAK
VISSTGGSVY SSTRPNLSAM NVSGTGRSFH SFPSSVPGDD KIVAEKFPRG NNEIRESEPS
CTHLNGVEKS FGNSAFPAEQ FESRKACLDD MDDDDILENI DVDQIVMEHY HSTSTPQPSV
SNFSLRTPPV DRSASRLEEE CNLPPELCSN CSHGIKLGLC PEASTHVEQM KDVLLAISNE
LLDDATDLSP DRVGQLRQER LRLKKQIQQL ENHIRDKESQ KSQFLSSTAT RIFQYETPKS
TNYKMDQPQT DFRAHVSDQG RYACDSWNTP RDSSFSVDRY GLSSAPVERE QYVPKIIDVT
YTEGSNDKKW SSREFPWTRK LEVNNKKVFG NHSFRPNQRE IINATMSGSD VFVLMPTGGG
KSLTYQLPAL ICGGITLVIS PLVSLIQDQI MNLLQANIPA ASLSAGMEWA EQLKIFQELN
SEHSKYKLLY VTPEKVAKSD SLLRHLENLN SRGLLARFVI DEAHCVSQWG HDFRPDYQSL
GILKQKFPNI PVLALTATAT ASVKEDVVQA LGLVNCVVFR QSFNRPNLWY SVVPKTKKCL
EDIDKFIKEN HFDECGIIYC LSRMDCEKVS ERLQEFGHKA AFYHGSMEPE QRAFIQTQWS
KDEINIICAT VAFGMGINKP DVRFVIHHSL PKSIEGYHQE CGRAGRDGQR SSCVLYYGYG
DYIRVKHMIS QGGVDQSPMA TGYNRVASSG RLLETNTENL LRMVRYCENE VECRRFLQLV
HLGEKFDSTN CKKTCDNCCS SQSLIDKDVT LITRQLVELV KQTGERFSSA HILEVYRGSL
NQMVKKHRHE TLQFHGAGKH LSKIEVSRIL HYLVTEDILV EDVRKSDMYG SVSSLLQVNN
AKATILFSGS QTIVMKFPSS VKVLKPSKQG ATAAKGPLTS EKQSTLPLTT EDAPPKDVNL
SANMYTALRK LRTALVKEAP DGVMAYHIFI NSTLQQISRR IPRTKEELLE INGLGKAKVS
KYGDQLLETI ETTVNEYYGT NKKDSIISND SPDSGKRRRD ENISPNVAED DDFEVSPSQS
CKKTVRNKSN EVLHGECIDG DRRGMELDFD FKDEDGSEIR PEGRVLPW
