SGS1_YEAST
ID SGS1_YEAST Reviewed; 1447 AA.
AC P35187; D6W014;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=ATP-dependent helicase SGS1 {ECO:0000303|PubMed:7969174};
DE EC=3.6.4.12 {ECO:0000269|PubMed:9545297};
DE AltName: Full=Helicase TPS1;
GN Name=SGS1 {ECO:0000303|PubMed:7969174}; Synonyms=TPS1;
GN OrderedLocusNames=YMR190C {ECO:0000312|SGD:S000004802};
GN ORFNames=YM9646.02C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=7969174; DOI=10.1128/mcb.14.12.8391-8398.1994;
RA Gangloff S., McDonald J.P., Bendixen C., Arthur L., Rothstein R.;
RT "The yeast type I topoisomerase Top3 interacts with Sgs1, a DNA helicase
RT homolog: a potential eukaryotic reverse gyrase.";
RL Mol. Cell. Biol. 14:8391-8398(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=7736577; DOI=10.1016/0092-8674(95)90335-6;
RA Watt P.M., Louis E.J., Borts R.H., Hickson I.D.;
RT "Sgs1: a eukaryotic homolog of E. coli RecQ that interacts with
RT topoisomerase II in vivo and is required for faithful chromosome
RT segregation.";
RL Cell 81:253-260(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Romeo A.M., Kleff S., Sternglanz R.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DNA-BINDING.
RX PubMed=9545297; DOI=10.1074/jbc.273.16.9644;
RA Bennett R.J., Sharp J.A., Wang J.C.;
RT "Purification and characterization of the Sgs1 DNA helicase activity of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:9644-9650(1998).
RN [7]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10640278;
RA Frei C., Gasser S.M.;
RT "The yeast Sgs1p helicase acts upstream of Rad53p in the DNA replication
RT checkpoint and colocalizes with Rad53p in S-phase-specific foci.";
RL Genes Dev. 14:81-96(2000).
RN [8]
RP INTERACTION WITH MLH3 AND TOP3.
RX PubMed=12200140; DOI=10.1016/s0006-291x(02)02034-x;
RA Wang T.-F., Kung W.M.;
RT "Supercomplex formation between Mlh1-Mlh3 and Sgs1-Top3 heterocomplexes in
RT meiotic yeast cells.";
RL Biochem. Biophys. Res. Commun. 296:949-953(2002).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLN-31; THR-980 AND GLU-987.
RX PubMed=12228808; DOI=10.1007/s00294-002-0319-6;
RA Kaliraman V., Brill S.J.;
RT "Role of SGS1 and SLX4 in maintaining rDNA structure in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 41:389-400(2002).
RN [10]
RP SUBUNIT.
RX PubMed=15889139; DOI=10.1038/sj.emboj.7600684;
RA Chang M., Bellaoui M., Zhang C., Desai R., Morozov P., Delgado-Cruzata L.,
RA Rothstein R., Freyer G.A., Boone C., Brown G.W.;
RT "RMI1/NCE4, a suppressor of genome instability, encodes a member of the
RT RecQ helicase/Topo III complex.";
RL EMBO J. 24:2024-2033(2005).
RN [11]
RP SUBUNIT.
RX PubMed=15899853; DOI=10.1128/mcb.25.11.4476-4487.2005;
RA Mullen J.R., Nallaseth F.S., Lan Y.Q., Slagle C.E., Brill S.J.;
RT "Yeast Rmi1/Nce4 controls genome stability as a subunit of the Sgs1-Top3
RT complex.";
RL Mol. Cell. Biol. 25:4476-4487(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP STRUCTURE BY NMR OF HRDC DOMAIN.
RX PubMed=10647186; DOI=10.1016/s0969-2126(00)88346-x;
RA Liu Z., Macias M.J., Bottomley M.J., Stier G., Linge J.P., Nilges M.,
RA Bork P., Sattler M.;
RT "The three-dimensional structure of the HRDC domain and implications for
RT the Werner and Bloom syndrome proteins.";
RL Structure 7:1557-1566(1999).
CC -!- FUNCTION: ATP-dependent DNA helicase able to unwind duplex DNA or
CC DNA- RNA heteroduplex (PubMed:9545297). Displacement of the DNA strand
CC occurs in the 3' to 5' direction with respect to the single-stranded
CC DNA flanking the duplex (PubMed:9545297). Acts as an integral component
CC of the S-phase checkpoint response, which arrests cells due to DNA
CC damage or blocked fork progression during DNA replication
CC (PubMed:10640278). Can create a deleterious topological substrate that
CC TOP3 preferentially resolves. The TOP3-SGS1 protein complex may
CC function as a eukaryotic reverse gyrase introducing positive supercoils
CC into extrachromosomal ribosomal DNA rings (PubMed:7969174). Together
CC with topoisomerase II has a role in chromosomal segregation
CC (PubMed:7736577). Maintains rDNA structure where it has a role in re-
CC starting stalled replication forks (PubMed:12228808).
CC {ECO:0000269|PubMed:10640278, ECO:0000269|PubMed:12228808,
CC ECO:0000269|PubMed:7736577, ECO:0000269|PubMed:7969174,
CC ECO:0000269|PubMed:9545297}.
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:0000269|PubMed:9545297};
CC -!- SUBUNIT: Heterodimer with TOP3 (PubMed:7969174, PubMed:15899853). Forms
CC a complex with TOP3 and RMI1 (PubMed:15889139). Forms a ternary complex
CC with a MLH1-MLH3 heterodimer (MutLbeta) during meiosis
CC (PubMed:12200140). Interacts with TOP2 (PubMed:7736577).
CC {ECO:0000269|PubMed:12200140, ECO:0000269|PubMed:15889139,
CC ECO:0000269|PubMed:15899853, ECO:0000269|PubMed:7736577,
CC ECO:0000269|PubMed:7969174}.
CC -!- INTERACTION:
CC P35187; P22216: RAD53; NbExp=3; IntAct=EBI-17059, EBI-17843;
CC P35187; P22336: RFA1; NbExp=5; IntAct=EBI-17059, EBI-14971;
CC P35187; Q02685: RMI1; NbExp=7; IntAct=EBI-17059, EBI-38690;
CC P35187; Q12306: SMT3; NbExp=3; IntAct=EBI-17059, EBI-17490;
CC P35187; P13099: TOP3; NbExp=6; IntAct=EBI-17059, EBI-19365;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10640278}.
CC Note=Localizes to S-phase-specific nuclear foci (PubMed:10640278).
CC {ECO:0000269|PubMed:10640278}.
CC -!- INDUCTION: Expression is regulated through the cell cycle with an
CC accumulation in S phase. {ECO:0000269|PubMed:10640278}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; U22341; AAB60289.1; -; Genomic_DNA.
DR EMBL; L07870; AAA35167.1; -; Genomic_DNA.
DR EMBL; Z47815; CAA87811.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10088.1; -; Genomic_DNA.
DR PIR; S50918; S50918.
DR RefSeq; NP_013915.1; NM_001182696.1.
DR PDB; 1D8B; NMR; -; A=1271-1351.
DR PDBsum; 1D8B; -.
DR AlphaFoldDB; P35187; -.
DR BMRB; P35187; -.
DR SMR; P35187; -.
DR BioGRID; 35368; 2345.
DR ComplexPortal; CPX-1071; RecQ helicase-Topo III complex.
DR DIP; DIP-2911N; -.
DR IntAct; P35187; 16.
DR MINT; P35187; -.
DR STRING; 4932.YMR190C; -.
DR iPTMnet; P35187; -.
DR MaxQB; P35187; -.
DR PaxDb; P35187; -.
DR PRIDE; P35187; -.
DR EnsemblFungi; YMR190C_mRNA; YMR190C; YMR190C.
DR GeneID; 855228; -.
DR KEGG; sce:YMR190C; -.
DR SGD; S000004802; SGS1.
DR VEuPathDB; FungiDB:YMR190C; -.
DR eggNOG; KOG0351; Eukaryota.
DR GeneTree; ENSGT00940000156800; -.
DR HOGENOM; CLU_001103_22_1_1; -.
DR InParanoid; P35187; -.
DR OMA; KACMFSS; -.
DR BioCyc; YEAST:G3O-32877-MON; -.
DR BRENDA; 3.6.4.12; 984.
DR EvolutionaryTrace; P35187; -.
DR PRO; PR:P35187; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P35187; protein.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IDA:SGD.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0051276; P:chromosome organization; IMP:SGD.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006265; P:DNA topological change; IDA:SGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IGI:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IGI:SGD.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IGI:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0010947; P:negative regulation of meiotic joint molecule formation; IGI:SGD.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IGI:SGD.
DR GO; GO:0000723; P:telomere maintenance; IGI:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR GO; GO:0031860; P:telomeric 3' overhang formation; IGI:SGD.
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; IPR022758; Helicase_Sgs1.
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; PF11408; Helicase_Sgs1; 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; SM00341; HRDC; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1447
FT /note="ATP-dependent helicase SGS1"
FT /id="PRO_0000205057"
FT DOMAIN 687..864
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 886..1035
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1272..1351
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 37..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 808..811
FT /note="DEAH box"
FT COMPBIAS 38..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1447
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 714..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 31
FT /note="Q->P: In allele sgs1-34; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12228808"
FT MUTAGEN 980
FT /note="T->I: In allele sgs1-35; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12228808"
FT MUTAGEN 987
FT /note="E->K: In allele sgs1-36; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:12228808"
FT HELIX 1274..1291
FT /evidence="ECO:0007829|PDB:1D8B"
FT STRAND 1292..1295
FT /evidence="ECO:0007829|PDB:1D8B"
FT HELIX 1303..1312
FT /evidence="ECO:0007829|PDB:1D8B"
FT HELIX 1317..1320
FT /evidence="ECO:0007829|PDB:1D8B"
FT HELIX 1321..1323
FT /evidence="ECO:0007829|PDB:1D8B"
FT HELIX 1328..1333
FT /evidence="ECO:0007829|PDB:1D8B"
FT HELIX 1334..1336
FT /evidence="ECO:0007829|PDB:1D8B"
FT HELIX 1338..1347
FT /evidence="ECO:0007829|PDB:1D8B"
FT TURN 1348..1350
FT /evidence="ECO:0007829|PDB:1D8B"
SQ SEQUENCE 1447 AA; 163837 MW; 0DC320B41756A3C3 CRC64;
MVTKPSHNLR REHKWLKETA TLQEDKDFVF QAIQKHIANK RPKTNSPPTT PSKDECGPGT
TNFITSIPAS GPTNTATKQH EVMQTLSNDT EWLSYTATSN QYADVPMVDI PASTSVVSNP
RTPNGSKTHN FNTFRPHMAS SLVENDSSRN LGSRNNNKSV IDNSSIGKQL ENDIKLEVIR
LQGSLIMALK EQSKLLLQKC SIIESTSLSE DAKRLQLSRD IRPQLSNMSI RIDSLEKEII
KAKKDGMSKD QSKGRSQVSS QDDNIISSIL PSPLEYNTSS RNSNLTSTTA TTVTKALAIT
GAKQNITNNT GKNSNNDSNN DDLIQVLDDE DDIDCDPPVI LKEGAPHSPA FPHLHMTSEE
QDELTRRRNM RSREPVNYRI PDRDDPFDYV MGKSLRDDYP DVEREEDELT MEAEDDAHSS
YMTTRDEEKE ENELLNQSDF DFVVNDDLDP TQDTDYHDNM DVSANIQESS QEGDTRSTIT
LSQNKNVQVI LSSPTAQSVP SNGQNQIGVE HIDLLEDDLE KDAILDDSMS FSFGRQHMPM
SHSDLELIDS EKENEDFEED NNNNGIEYLS DSDLERFDEE RENRTQVADI QELDNDLKII
TERKLTGDNE HPPPSWSPKI KREKSSVSQK DEEDDFDDDF SLSDIVSKSN LSSKTNGPTY
PWSDEVLYRL HEVFKLPGFR PNQLEAVNAT LQGKDVFVLM PTGGGKSLCY QLPAVVKSGK
THGTTIVISP LISLMQDQVE HLLNKNIKAS MFSSRGTAEQ RRQTFNLFIN GLLDLVYISP
EMISASEQCK RAISRLYADG KLARIVVDEA HCVSNWGHDF RPDYKELKFF KREYPDIPMI
ALTATASEQV RMDIIHNLEL KEPVFLKQSF NRTNLYYEVN KKTKNTIFEI CDAVKSRFKN
QTGIIYCHSK KSCEQTSAQM QRNGIKCAYY HAGMEPDERL SVQKAWQADE IQVICATVAF
GMGIDKPDVR FVYHFTVPRT LEGYYQETGR AGRDGNYSYC ITYFSFRDIR TMQTMIQKDK
NLDRENKEKH LNKLQQVMAY CDNVTDCRRK LVLSYFNEDF DSKLCHKNCD NCRNSANVIN
EERDVTEPAK KIVKLVESIQ NERVTIIYCQ DVFKGSRSSK IVQANHDTLE EHGIGKSMQK
SEIERIFFHL ITIRVLQEYS IMNNSGFASS YVKVGPNAKK LLTGKMEIKM QFTISAPNSR
PSTSSSFQAN EDNIPVIAQK STTIGGNVAA NPPRFISAKE HLRSYTYGGS TMGSSHPITL
KNTSDLRSTQ ELNNLRMTYE RLRELSLNLG NRMVPPVGNF MPDSILKKMA AILPMNDSAF
ATLGTVEDKY RRRFKYFKAT IADLSKKRSS EDHEKYDTIL NDEFVNRAAA SSNGIAQSTG
TKSKFFGANL NEAKENEQII NQIRQSQLPK NTTSSKSGTR SISKSSKKSA NGRRGFRNYR
GHYRGRK
