SRS2L_ARATH
ID SRS2L_ARATH Reviewed; 1147 AA.
AC D1KF50; F4JSH5; Q9SW14;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent DNA helicase SRS2-like protein At4g25120;
DE EC=3.6.4.12;
DE AltName: Full=AtSRS2;
GN Name=SRS2; OrderedLocusNames=At4g25120; ORFNames=F13M23.260;
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), FUNCTION, COFACTOR, AND MUTAGENESIS
RP OF LYS-273.
RX PubMed=19767619; DOI=10.1093/nar/gkp753;
RA Blanck S., Kobbe D., Hartung F., Fengler K., Focke M., Puchta H.;
RT "A SRS2 homolog from Arabidopsis thaliana disrupts recombinogenic DNA
RT intermediates and facilitates single strand annealing.";
RL Nucleic Acids Res. 37:7163-7176(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 REVIEW.
RX PubMed=21081662; DOI=10.1093/jxb/erq357;
RA Knoll A., Puchta H.;
RT "The role of DNA helicases and their interaction partners in genome
RT stability and meiotic recombination in plants.";
RL J. Exp. Bot. 62:1565-1579(2011).
CC -!- FUNCTION: ATP-dependent 3'- to 5'-DNA helicase that could disrupt
CC recombinogenic DNA intermediates and facilitate single strand
CC annealing. Unwinds nicked and partial Holliday junctions in vitro.
CC Anneals two single strands into a dsDNA molecule in vitro.
CC {ECO:0000269|PubMed:19767619}.
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;
CC Evidence={ECO:0000269|PubMed:19767619};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19767619};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D1KF50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D1KF50-2; Sequence=VSP_055611;
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36754.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ148553; ACY64665.1; -; mRNA.
DR EMBL; AL035523; CAB36754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161562; CAB79421.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85014.2; -; Genomic_DNA.
DR PIR; T05533; T05533.
DR RefSeq; NP_001320059.1; NM_001341722.1. [D1KF50-1]
DR AlphaFoldDB; D1KF50; -.
DR SMR; D1KF50; -.
DR STRING; 3702.AT4G25120.1; -.
DR PaxDb; D1KF50; -.
DR PRIDE; D1KF50; -.
DR ProteomicsDB; 226737; -. [D1KF50-1]
DR EnsemblPlants; AT4G25120.1; AT4G25120.1; AT4G25120. [D1KF50-1]
DR GeneID; 828615; -.
DR Gramene; AT4G25120.1; AT4G25120.1; AT4G25120. [D1KF50-1]
DR KEGG; ath:AT4G25120; -.
DR Araport; AT4G25120; -.
DR TAIR; locus:2117303; AT4G25120.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_004585_0_0_1; -.
DR OMA; IKECHNE; -.
DR OrthoDB; 245505at2759; -.
DR PRO; PR:D1KF50; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; D1KF50; baseline and differential.
DR Genevisible; D1KF50; AT.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:TAIR.
DR GO; GO:0006310; P:DNA recombination; IDA:TAIR.
DR GO; GO:0036292; P:DNA rewinding; IDA:TAIR.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1147
FT /note="ATP-dependent DNA helicase SRS2-like protein
FT At4g25120"
FT /id="PRO_0000430141"
FT DOMAIN 246..548
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 549..860
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT VAR_SEQ 396..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055611"
FT MUTAGEN 273
FT /note="K->R: Abolishes DNA-ligase unwinding activity."
FT /evidence="ECO:0000269|PubMed:19767619"
SQ SEQUENCE 1147 AA; 129430 MW; 36113DB18DB7695B CRC64;
MENLPPNRGM WNQEYSHGRI SQSFRSAKPL LDRKRPIENA PNSSNPLPQR MKESMDTESV
SHNINFNSTP LMELSANTPY KRLKPEIESY ADGHPCGLRT PPPRFDLDKE IINGFQTDIY
ADVGSLSEAF VTPLKEPERV TLSNGCSTSS ILDDDFDDSI LEEIDLICEQ SARKAACQTP
TTSIYQTPSK DNKSSDPKAS LDFRDVEKFE PDSNVKLKLD EETPTIAADP ALLNSMPDEC
SKYMLSLNDR QRDAACSNIS TPLMVIAGPG SGKTSTMVGR VLVLLNEGLL PSNILAMTFT
KAATSEMRER IGKSAGKKAA KDITISTFHS FSLQLCRMHA DKLQRTSEFS VYGHGQQRRA
IIEAVRLYEE EKKNGSKTSV PCESGEGLNG AGAGAVCPEY AKDLSKKWQK FVTQGKASGK
SPEQCRKMGN EIGAKILGNY NDILKACDAL DYHDLISCSV TLLSDFPEVF KECQDTWKAI
IVDEFQDTST MQYKLLRMLG SHNHITIVGD DDQSIFGFNG ADSSGFDSFR RDFPNYKEVR
LIKNYRSSRH IVEAASSIIK NNTKRCQSKS ISSENSQGSK ITVKECHNEE AQCAYVIDKI
IEITNDGSTP CCSHGDIAIL YRRQVSGKVF QNAFRQRKIP FNVHGVAFYR KKVVQVILAM
LKTTFSECDD ASYRRVFKAL LPFEKEEKKR IIEHIEKIST SRKCSFISAA SDIFNAKISG
TFKRSQLTQG RKVLQTLDMV AKLVDREQSL SAVVTCVANM IPQKYLLEQR AVVDNDGGKL
LNEDNDLRSV LQYLMDDVAE FISTHCTTTE EEDAIKEKKG CNQLHSFINY ISERETENFR
SRRRDNENSV TLTTIHQSKG LEWDIVFIVK ANENEIPLLH ESNGNASESG TSLEEERRLL
YVAMTRARKK LFFLYVTVDS NWQVLQPSRF LKEIPGHLLQ GDMSVNDCRK VHENLPNKTE
QSVSSFGTDI KHEESKLTDN DVMNIPEDYA SEESIAAYAL NGNNFLKRFD VEVRSVVSHL
FHNWAKKQAF QEPKRLIDKV RFVIGERLAI KKNKHKDVLR ALKSSLTSEE AFQYAEHVLR
WEQLPADTRA HIVREKQEHF QKLRIENSMG TSEATSKQIA FLHSLGCTVV PTSRLHASRL
IEQYKSL
