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 01-MAY-2013, entry version 134.
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 204511 / S288c / AB972;
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 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 Q12306:SMT3; NbExp=3; IntAct=EBI-17059, EBI-17490;
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 DIP; DIP-2911N; -.
DR IntAct; P35187; 9.
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; EOG4XSPZ5; -.
DR EvolutionaryTrace; P35187; -.
DR NextBio; 978762; -.
DR Genevestigator; P35187; -.
DR GermOnline; YMR190C; Saccharomyces cerevisiae.
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:0006268; P:DNA unwinding involved in 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: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 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; 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; HRDC_like; 1.
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
//
