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Database: UniProt
Entry: P35187
LinkDB: P35187
Original site: P35187 
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   16-APR-2014, entry version 142.
DE   RecName: Full=ATP-dependent helicase SGS1;
DE            EC=3.6.4.-;
DE   AltName: Full=Helicase TPS1;
GN   Name=SGS1; Synonyms=TPS1; OrderedLocusNames=YMR190C;
GN   ORFNames=YM9646.02C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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;
RA   Gangloff S., McDonald J.P., Bendixen C., Arthur L., Rothstein R.;
RT   "The yeast type I topoisomerase Top3 interacts with Sgs1, a DNA
RT   helicase 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.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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
RT   heterocomplexes in meiotic yeast cells.";
RL   Biochem. Biophys. Res. Commun. 296:949-953(2002).
RN   [7]
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   [8]
RP   SUBUNIT.
RX   PubMed=15889139; DOI=10.1038/sj.emboj.7600684;
RA   Chang M., Bellaoui M., Zhang C., Desai R., Morozov P.,
RA   Delgado-Cruzata L., Rothstein R., Freyer G.A., Boone C., Brown G.W.;
RT   "RMI1/NCE4, a suppressor of genome instability, encodes a member of
RT   the RecQ helicase/Topo III complex.";
RL   EMBO J. 24:2024-2033(2005).
RN   [9]
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-
RT   Top3 complex.";
RL   Mol. Cell. Biol. 25:4476-4487(2005).
RN   [10]
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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
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
RT   for the Werner and Bloom syndrome proteins.";
RL   Structure 7:1557-1566(1999).
CC   -!- FUNCTION: Interacts with topoisomerases II and TOP3. Could create
CC       a deleterious topological substrate that TOP3 preferentially
CC       resolves. The TOP3-SGS1 protein complex may function as a
CC       eukaryotic reverse gyrase introducing positive supercoils into
CC       extrachromosomal ribosomal DNA rings. Together with topoisomerase
CC       II has a role in chromosomal segregation. Maintains rDNA structure
CC       where it has a role in re-starting stalled replication forks.
CC   -!- SUBUNIT: Heterodimer with TOP3. Forms a complex with TOP3 and
CC       RMI1. Forms a ternary complex with a MLH1-MLH3 heterodimer
CC       (MutLbeta) during meiosis. Interacts with TOP2.
CC   -!- INTERACTION:
CC       P22216:RAD53; NbExp=3; IntAct=EBI-17059, EBI-17843;
CC       P22336:RFA1; NbExp=5; IntAct=EBI-17059, EBI-14971;
CC       Q02685:RMI1; NbExp=2; IntAct=EBI-17059, EBI-38690;
CC       Q12306:SMT3; NbExp=3; IntAct=EBI-17059, EBI-17490;
CC       P13099:TOP3; NbExp=3; IntAct=EBI-17059, EBI-19365;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 HRDC domain.
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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   ProteinModelPortal; P35187; -.
DR   SMR; P35187; 656-1193, 1271-1351.
DR   BioGrid; 35368; 450.
DR   DIP; DIP-2911N; -.
DR   IntAct; P35187; 12.
DR   MINT; MINT-442647; -.
DR   STRING; 4932.YMR190C; -.
DR   PaxDb; P35187; -.
DR   PeptideAtlas; P35187; -.
DR   EnsemblFungi; YMR190C; YMR190C; YMR190C.
DR   GeneID; 855228; -.
DR   KEGG; sce:YMR190C; -.
DR   CYGD; YMR190c; -.
DR   SGD; S000004802; SGS1.
DR   eggNOG; COG0514; -.
DR   GeneTree; ENSGT00550000074520; -.
DR   HOGENOM; HOG000141897; -.
DR   KO; K10901; -.
DR   OMA; TIFEICD; -.
DR   OrthoDB; EOG7CRTZ8; -.
DR   BioCyc; YEAST:G3O-32877-MONOMER; -.
DR   EvolutionaryTrace; P35187; -.
DR   NextBio; 978762; -.
DR   Genevestigator; P35187; -.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0031422; C:RecQ helicase-Topo III complex; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:SGD.
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; IGI:SGD.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD.
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; IMP:SGD.
DR   GO; GO:0031292; P:gene conversion at mating-type locus, DNA double-strand break processing; IGI:SGD.
DR   GO; GO:0031573; P:intra-S DNA damage checkpoint; IMP: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: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:0001302; P:replicative cell aging; IMP: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; DNA/RNA_helicase_DEAD/DEAH_N.
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.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF11408; Helicase_Sgs1; 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; 3.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1447       ATP-dependent helicase SGS1.
FT                                /FTId=PRO_0000205057.
FT   DOMAIN      687    864       Helicase ATP-binding.
FT   DOMAIN      886   1035       Helicase C-terminal.
FT   DOMAIN     1272   1351       HRDC.
FT   NP_BIND     714    721       ATP (By similarity).
FT   MOTIF       808    811       DEAH box.
FT   COMPBIAS    631    639       Asp/Glu-rich (highly acidic).
FT   MUTAGEN      31     31       Q->P: In allele sgs1-34; temperature-
FT                                sensitive.
FT   MUTAGEN     980    980       T->I: In allele sgs1-35; temperature-
FT                                sensitive.
FT   MUTAGEN     987    987       E->K: In allele sgs1-36; temperature-
FT                                sensitive.
FT   HELIX      1274   1291
FT   STRAND     1292   1295
FT   HELIX      1303   1312
FT   HELIX      1317   1320
FT   HELIX      1321   1323
FT   HELIX      1328   1333
FT   HELIX      1334   1336
FT   HELIX      1338   1347
FT   TURN       1348   1350
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
//
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