RECQ2_ARATH
ID RECQ2_ARATH Reviewed; 705 AA.
AC Q9FT73; A8MRK2; Q9SHE4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-dependent DNA helicase Q-like 2;
DE EC=3.6.4.12 {ECO:0000305|PubMed:18419780};
DE AltName: Full=RecQ-like protein 2 {ECO:0000303|PubMed:11058127};
DE Short=AtRQ2 {ECO:0000303|PubMed:16371241};
DE Short=AtRecQ2 {ECO:0000303|PubMed:16371241};
DE Short=AtRecQl2 {ECO:0000303|PubMed:11058127};
GN Name=RECQL2 {ECO:0000303|PubMed:11058127};
GN Synonyms=MED34 {ECO:0000303|PubMed:17560376},
GN MED34_1 {ECO:0000303|PubMed:22021418}, RECQ2 {ECO:0000303|PubMed:16371241},
GN RQL2; OrderedLocusNames=At1g31360 {ECO:0000312|Araport:AT1G31360};
GN ORFNames=T19E23.16 {ECO:0000312|EMBL:AAF24590.1};
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), TISSUE SPECIFICITY, AND INTERACTION
RP WITH WEX.
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.
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 IDENTIFICATION BY MASS SPECTROMETRY, AND NOMENCLATURE.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-117, AND COFACTOR.
RX PubMed=18419780; DOI=10.1111/j.0960-7412.2008.03511.x;
RA Kobbe D., Blanck S., Demand K., Focke M., Puchta H.;
RT "AtRECQ2, a RecQ helicase homologue from Arabidopsis thaliana, is able to
RT disrupt various recombinogenic DNA structures in vitro.";
RL Plant J. 55:397-405(2008).
RN [8]
RP FUNCTION.
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 [9]
RP NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [10]
RP FUNCTION.
RX PubMed=23771268; DOI=10.1038/ncomms3024;
RA Klaue D., Kobbe D., Kemmerich F., Kozikowska A., Puchta H., Seidel R.;
RT "Fork sensing and strand switching control antagonistic activities of RecQ
RT helicases.";
RL Nat. Commun. 4:2024-2024(2013).
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 that may play a role in the repair of DNA
CC (PubMed:18419780, PubMed:19755539). Its DNA unwinding activity in vitro
CC is dependent on magnesium, and ATP or dATP (PubMed:18419780,
CC PubMed:19755539). Can use GTP/dGTP, CTP/dCTP or UTP/dUTP as nucleotide
CC cofactors (PubMed:18419780, PubMed:19755539). Catalyzes Holliday
CC junction branch migration and replication fork regression
CC (PubMed:19755539, PubMed:23771268). Disrupts D-loop structures
CC (PubMed:18419780). {ECO:0000269|PubMed:18419780,
CC ECO:0000269|PubMed:19755539, ECO:0000269|PubMed:23771268}.
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 Evidence={ECO:0000305|PubMed:18419780};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:18419780};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18419780};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18419780};
CC -!- SUBUNIT: Interacts with WEX. {ECO:0000269|PubMed:11058127}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FT73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FT73-2; Sequence=VSP_039139;
CC -!- TISSUE SPECIFICITY: Expressed in shoots and flowers (PubMed:11058127,
CC PubMed:12856935). Expressed in young leaves, inflorescences, roots,
CC shoot apical meristem, young siliques, and mature green siliques
CC (PubMed:12856935). {ECO:0000269|PubMed:11058127,
CC ECO:0000269|PubMed:12856935}.
CC -!- MISCELLANEOUS: Baeckstroem et al identified RECQL2 in a Mediator
CC complex pull-down assay and suggested that RECQL2 could be a plant
CC specific component of the Mediator complex (PubMed:17560376). However,
CC no experimental evidence has been brought so far to confirm this
CC hypothesis (Probable). {ECO:0000269|PubMed:17560376, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24590.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ404471; CAC14866.1; -; mRNA.
DR EMBL; AC007654; AAF24590.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31346.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31347.1; -; Genomic_DNA.
DR RefSeq; NP_001077639.1; NM_001084170.2. [Q9FT73-2]
DR RefSeq; NP_001319121.1; NM_001332956.1. [Q9FT73-1]
DR AlphaFoldDB; Q9FT73; -.
DR SMR; Q9FT73; -.
DR BioGRID; 25261; 1.
DR IntAct; Q9FT73; 2.
DR STRING; 3702.AT1G31360.1; -.
DR iPTMnet; Q9FT73; -.
DR PaxDb; Q9FT73; -.
DR PRIDE; Q9FT73; -.
DR EnsemblPlants; AT1G31360.1; AT1G31360.1; AT1G31360. [Q9FT73-1]
DR EnsemblPlants; AT1G31360.2; AT1G31360.2; AT1G31360. [Q9FT73-2]
DR GeneID; 840026; -.
DR Gramene; AT1G31360.1; AT1G31360.1; AT1G31360. [Q9FT73-1]
DR Gramene; AT1G31360.2; AT1G31360.2; AT1G31360. [Q9FT73-2]
DR KEGG; ath:AT1G31360; -.
DR Araport; AT1G31360; -.
DR TAIR; locus:2197555; AT1G31360.
DR eggNOG; KOG0353; Eukaryota.
DR InParanoid; Q9FT73; -.
DR PhylomeDB; Q9FT73; -.
DR PRO; PR:Q9FT73; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FT73; baseline and differential.
DR Genevisible; Q9FT73; AT.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009378; F:four-way junction 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; 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; 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; 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; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; DNA-binding; Helicase;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..705
FT /note="ATP-dependent DNA helicase Q-like 2"
FT /id="PRO_0000394133"
FT DOMAIN 98..273
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 298..450
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 591..670
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 668..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..30
FT /evidence="ECO:0000255"
FT MOTIF 217..220
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 668..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039139"
FT MUTAGEN 117
FT /note="K->M: Loss of ATPase or helicase activity."
FT /evidence="ECO:0000269|PubMed:18419780"
SQ SEQUENCE 705 AA; 79369 MW; 7976A97A8015DD90 CRC64;
MESEAIQEDL QNLDVELKDV QGQISALIEH QDRLYERKSE LKTLLKALAA SGSPVASSGG
SSAIENWSET FEWDSRADDV RFNVFGISKY RANQKEIINA IMTGRDVLVI MAAGGGKSLC
YQLPAMLRGG TTLVVSPLLS LIQDQVMGLA ALGISAYMLT STSGKENEKF VYKALEKGED
DLKILYVTPE KVSKSKRFMS KLEKCHNAGR LSLISIDEAH CCSQWGHDFR PDYKNLSILK
TQFPKVPMVA LTATATQKVQ NDLIEMLHIP KCVKFVSSVN RPNLFYSVRE KSAVGKLVVD
EIAEFIRESY SNNESGIVYC FSRKECEQIA GDLRERGISA DYYHADMDAN MREKVHMRWS
KNKLQVIVGT VAFGMGINKP DVRFVIHHSL SKSMETYYQE SGRAGRDGLP SECILFFRSA
DVPRQSSMVF YEYSGLQNLY DIVRYCQSKT KCRRSAFFRH FGEPSQDCNG MCDNCALSSE
VKEVDVSDLS KLVVSMVQET QAKDQRVTML QLGDKLRNKH KDLIAELKRD EVEHLVIKLI
VDSVLKEEFQ HTPYSTNAYV TMGPLANQLL QGRKTIKMET SSRQTKKLKR SITFSGLELK
LDELRKEISA ADGSILPHTV LSTQQIGSIS SQKPVSLQEL ESIIGKLKTE KYGDRILEEV
MRHEAVSEQL VEDPTKEETC KSRLRKRAKT QKDVVLVESS GEEEA
