RQL4B_ARATH
ID RQL4B_ARATH Reviewed; 1150 AA.
AC Q9FT70; Q9C959;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP-dependent DNA helicase Q-like 4B;
DE EC=3.6.4.12;
DE AltName: Full=RecQ-like protein 4B;
DE Short=AtRecQ4B;
DE Short=AtRecQl4B;
GN Name=RECQL4B; Synonyms=RECQ4B, RQL4B; OrderedLocusNames=At1g60930;
GN ORFNames=T7P1.7;
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 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 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 [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 (By similarity). Required to promote but not to suppress crossovers.
CC {ECO:0000250, ECO:0000269|PubMed:18000056}.
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 roots, seedlings, shoots, shoot
CC apical mersitem, flowers, and siliques. {ECO:0000269|PubMed:11058127,
CC ECO:0000269|PubMed:12856935}.
CC -!- INDUCTION: Repressed by cold. {ECO:0000269|PubMed:12856935}.
CC -!- DISRUPTION PHENOTYPE: Not mutagen-sensitive, and impaired in
CC hyperrecombination (HR). {ECO:0000269|PubMed:18000056}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51646.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51646.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ404474; CAC14869.1; -; mRNA.
DR EMBL; AC018908; AAG51646.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33749.1; -; Genomic_DNA.
DR PIR; G96634; G96634.
DR RefSeq; NP_176289.7; NM_104773.7.
DR AlphaFoldDB; Q9FT70; -.
DR SMR; Q9FT70; -.
DR STRING; 3702.AT1G60930.1; -.
DR iPTMnet; Q9FT70; -.
DR PaxDb; Q9FT70; -.
DR PRIDE; Q9FT70; -.
DR ProteomicsDB; 228235; -.
DR GeneID; 842384; -.
DR KEGG; ath:AT1G60930; -.
DR Araport; AT1G60930; -.
DR TAIR; locus:2206031; AT1G60930.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_276670_0_0_1; -.
DR InParanoid; Q9FT70; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q9FT70; -.
DR PRO; PR:Q9FT70; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FT70; baseline and differential.
DR Genevisible; Q9FT70; 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:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IMP: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; 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; IPR001763; Rhodanese-like_dom.
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; 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; Coiled coil; Helicase; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1150
FT /note="ATP-dependent DNA helicase Q-like 4B"
FT /id="PRO_0000394530"
FT DOMAIN 478..653
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 678..823
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1029..1111
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 124..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 327..361
FT /evidence="ECO:0000255"
FT MOTIF 597..600
FT /note="DEAH box"
FT COMPBIAS 416..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1150 AA; 128577 MW; 15E3054C24E8D005 CRC64;
MVVTRGDKFA GSSLACKSMI GANKMSGSHL HEVNNSRSHF PQTNWLKVAK AFECIPSLNK
FMGSNFLYSL ESQKLGRDRE MAARSIENIA PVTVQTLARP QIEKAWCTLI NLSINNTYLR
PGITPAIDND STSRTSSTKG STFKVTSNAD GSFCAHNHPE HSQRSVRGTA KSIDSFSSSS
VGDNKIIIDK VPRVNYEVRD SVTVTNGMEM PPIKNSAQLA RPVEPREVSL GEIDYDDIME
IIDVDQIAME HCPSTCTKQP SVSKFVDIFT SRREEEQGLP PEICSNCSHG IKLGLCPEAS
THVEQMKDTL LAISNEILDN TYDLGPDHVE QLHQKRLLLK KQIQQLEILI HNKERKKSQC
LVSIPSHNTQ YETPQTTNLE VVYGQTDSPT HVKEQGRCVT DNWNMPRDYL VSKERYDISS
GSEEREQSVS EVIDVTDTES SNDKKWTSSD FPWTKNLEVY NKLVFGNHSF RPNQREIINA
TMSGCDVFVL MPTGGGKSLT YQLPALLCAG ITLVISPLVS LIQDQIMNLL QTNISAASLS
AGMEWAEQLE ILQELSSEKS KYKLLYVTPE KVAKSESLLR HLEILNSRSL LARFVIDEAH
CVSQWGHDFR PDYQGLGVLK QKFPNIPMLA LTATATTSVK EDVVQALGLV NCVVFRQSFN
RPNLWYSVVP KTNKCLEDID KFIRENHFDE CGIIYCLSRM DCEKVTEALR VFGHKAAFYH
GSMDPGKRAF VQKQWSKDEI NIICATVAFG MGINKPDVRF VIHHSLPKSI EGYHQECGRA
GRDGQRSSCV LYYSYTDYIR VKHMISQGGL GQGQMKMGYN CKASSGRMLE TNTENLLRMV
SYCENEVDCR RFLQLVHLGE KFDSTNCKNT CDNCSSSKIL IDKDVTVIAR QLVALVKLTG
ERFSSAHIVE IYRGSLNQSV KRNRQDTLHL HGAGKHLTKS EASRILHYLV TEDILAEGVK
KSELYGSVSS LLKVNRSKAA SLLSGGQSIT MRFPSTIKVS KQSKSTANPA KVPLKQTTLP
MAKAAPQDSN LSGILLTALK NLRTDIVKES PDLVMAYHIF GNATLKEISK RLPRTKEELL
DINGLGKAKV SKYGDRLLET IDSTINDHYK TRPGSGKRRR DENVNPNVAE DDDPDWSASQ
SHKKVVKNKK
