RQSIM_ARATH
ID RQSIM_ARATH Reviewed; 858 AA.
AC Q9FT69;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ATP-dependent DNA helicase Q-like SIM;
DE EC=3.6.4.12;
DE AltName: Full=RecQ-like protein SIM;
DE Short=AtRecQsim;
DE Short=Similar to RecQ protein;
GN Name=RECQSIM; OrderedLocusNames=At5g27680; ORFNames=T1G16.10;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, AND 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 [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: Plant specific 3'-5' DNA helicase that may play a role in the
CC repair of DNA. {ECO:0000269|PubMed:12856935}.
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 and seedlings, and, to a
CC lower extent, in leaves, shoots, shoot apical mersitem, inflorescences,
CC flowers, siliques and seeds. {ECO:0000269|PubMed:11058127,
CC ECO:0000269|PubMed:12856935}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ404475; CAC14870.1; -; mRNA.
DR EMBL; AC007478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93714.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69089.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69091.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69093.1; -; Genomic_DNA.
DR EMBL; AY059754; AAL24102.1; -; mRNA.
DR EMBL; AY133823; AAM91757.1; -; mRNA.
DR RefSeq; NP_001330792.1; NM_001344027.1.
DR RefSeq; NP_001330794.1; NM_001344029.1.
DR RefSeq; NP_001330796.1; NM_001344028.1.
DR RefSeq; NP_568499.1; NM_122650.5.
DR AlphaFoldDB; Q9FT69; -.
DR SMR; Q9FT69; -.
DR BioGRID; 18104; 1.
DR IntAct; Q9FT69; 1.
DR STRING; 3702.AT5G27680.1; -.
DR PaxDb; Q9FT69; -.
DR PRIDE; Q9FT69; -.
DR ProteomicsDB; 228252; -.
DR EnsemblPlants; AT5G27680.1; AT5G27680.1; AT5G27680.
DR EnsemblPlants; AT5G27680.2; AT5G27680.2; AT5G27680.
DR EnsemblPlants; AT5G27680.3; AT5G27680.3; AT5G27680.
DR EnsemblPlants; AT5G27680.4; AT5G27680.4; AT5G27680.
DR GeneID; 832830; -.
DR Gramene; AT5G27680.1; AT5G27680.1; AT5G27680.
DR Gramene; AT5G27680.2; AT5G27680.2; AT5G27680.
DR Gramene; AT5G27680.3; AT5G27680.3; AT5G27680.
DR Gramene; AT5G27680.4; AT5G27680.4; AT5G27680.
DR KEGG; ath:AT5G27680; -.
DR Araport; AT5G27680; -.
DR TAIR; locus:2180255; AT5G27680.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_008232_0_0_1; -.
DR InParanoid; Q9FT69; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q9FT69; -.
DR BRENDA; 3.6.4.12; 399.
DR PRO; PR:Q9FT69; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FT69; baseline and differential.
DR Genevisible; Q9FT69; 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; 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: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; IDA: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; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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; SSF46934; SSF46934; 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; PS50030; UBA; 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..858
FT /note="ATP-dependent DNA helicase Q-like SIM"
FT /id="PRO_0000394532"
FT DOMAIN 2..44
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 177..353
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 491..627
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 402..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 288..291
FT /note="DEAH box"
FT COMPBIAS 402..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..850
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 858 AA; 97466 MW; BA972C23D84D3E27 CRC64;
MDLSSDQLVM KIVEMGFEKL DALEAVKAVG GKSCDDAVEY ILKGNHRTGG FKPASLLCSS
GSNKILGKRA MPSSFSSSES KRQSSLLDHF RSVNQNKKKG DTFGTVEVDS QLETVSEHSE
EVRKSLAPVF MESSCFPEGQ LLNGCSEASS SWEKRVNSIL RNRFGISSLR SFQREALSTW
VAHKDCLVLA ATGSGKSLCF QIPALLTGKV VVVISPLISL MHDQCLKLSR HKVSACFLGS
GQLDNCIEEK AMQGMYQIIY VCPETVVRLI KPLQKLAKTH GIALFAIDEA HCVSKWGHDF
RPHYRKLSVL RENFCASNLE FLEYDVPIMA LTATATVNVQ EDILESLHLS KETKIVLTSF
FRPNLQFSVK HSRTKFASSY AKDFQNLVDL YSEKKNSTGK KLAVISRESE EQTDFGSHDS
ENIHETDYDE DEEDQENSLA KKNSSNGKEL SEAYLEDETD IFQSVDDWDV ACGEFCAMPS
CELLEIPVPS EKQKDLEGLT IIYVPTRKES VNIAKYLCGV GLKAAAYNAS LPKKHLRQVH
QDFHDNKLQV VVATIAFGMG IDKKNVRKII HYGWLQSLEA YYQEAGRAGR DGELAECVLY
ADLSRAPTLL PSRRSKEQTE QAYKMLSDCF RYGMNTSQCR AKILVEYFGE EFSSKKCNSC
DVCTEGPPEL VDVREEANLL FQVITAFHLQ VDNDSEHAPY EDYGLGNSKQ NKLSHKPNLL
FFISKLREQC EKFKETDCLW WKGLARIMEA EGYIKEMDNK DRRVEIKFIQ PTEKGKKQLD
FQDDKPLYVY PEADMLLSLK QDRTYSGFSE WGKGWADPEI RRQRLERRER KPRRERKPRK
KRTRGRSSTK LHPWRSKE
