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Protein

ATP-dependent helicase SGS1

Gene

SGS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase able to unwind duplex DNA or DNA- RNA heteroduplex (PubMed:9545297). Displacement of the DNA strand occurs in the 3' to 5' direction with respect to the single-stranded DNA flanking the duplex (PubMed:9545297). Acts as an integral component of the S-phase checkpoint response, which arrests cells due to DNA damage or blocked fork progression during DNA replication (PubMed:10640278). Can create a deleterious topological substrate that TOP3 preferentially resolves. The TOP3-SGS1 protein complex may function as a eukaryotic reverse gyrase introducing positive supercoils into extrachromosomal ribosomal DNA rings (PubMed:7969174). Together with topoisomerase II has a role in chromosomal segregation (PubMed:7736577). Maintains rDNA structure where it has a role in re-starting stalled replication forks (PubMed:12228808).5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi714 – 721ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

  • chromosome organization Source: SGD
  • DNA double-strand break processing Source: SGD
  • DNA duplex unwinding Source: SGD
  • DNA topological change Source: SGD
  • DNA unwinding involved in DNA replication Source: SGD
  • double-strand break repair via homologous recombination Source: SGD
  • gene conversion at mating-type locus, DNA double-strand break processing Source: SGD
  • intra-S DNA damage checkpoint Source: SGD
  • meiotic chromosome segregation Source: SGD
  • meiotic DNA double-strand break processing Source: SGD
  • mitotic sister chromatid segregation Source: SGD
  • negative regulation of meiotic joint molecule formation Source: SGD
  • regulation of reciprocal meiotic recombination Source: SGD
  • replicative cell aging Source: SGD
  • telomere maintenance Source: SGD
  • telomere maintenance via recombination Source: SGD
  • telomeric 3' overhang formation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32877-MONOMER.
BRENDAi3.6.4.12. 984.
ReactomeiR-SCE-3108214. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent helicase SGS11 Publication (EC:3.6.4.121 Publication)
Alternative name(s):
Helicase TPS1
Gene namesi
Name:SGS11 Publication
Synonyms:TPS1
Ordered Locus Names:YMR190CImported
ORF Names:YM9646.02C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR190C.
SGDiS000004802. SGS1.

Subcellular locationi

  • Nucleusnucleolus 1 Publication

  • Note: Localizes to S-phase-specific nuclear foci (PubMed:10640278).1 Publication

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nucleolus Source: SGD
  • RecQ helicase-Topo III complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31Q → P in allele sgs1-34; temperature-sensitive. 1 Publication1
Mutagenesisi980T → I in allele sgs1-35; temperature-sensitive. 1 Publication1
Mutagenesisi987E → K in allele sgs1-36; temperature-sensitive. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050571 – 1447ATP-dependent helicase SGS1Add BLAST1447

Proteomic databases

MaxQBiP35187.
PRIDEiP35187.

PTM databases

iPTMnetiP35187.

Expressioni

Inductioni

Expression is regulated through the cell cycle with an accumulation in S phase.1 Publication

Interactioni

Subunit structurei

Heterodimer with TOP3 (PubMed:7969174, PubMed:15899853). Forms a complex with TOP3 and RMI1 (PubMed:15889139). Forms a ternary complex with a MLH1-MLH3 heterodimer (MutLbeta) during meiosis (PubMed:12200140). Interacts with TOP2 (PubMed:7736577).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD53P222163EBI-17059,EBI-17843
RFA1P223365EBI-17059,EBI-14971
RMI1Q026852EBI-17059,EBI-38690
SMT3Q123063EBI-17059,EBI-17490
TOP3P130993EBI-17059,EBI-19365

Protein-protein interaction databases

BioGridi35368. 450 interactors.
DIPiDIP-2911N.
IntActiP35187. 12 interactors.
MINTiMINT-442647.

Structurei

Secondary structure

11447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1274 – 1291Combined sources18
Beta strandi1292 – 1295Combined sources4
Helixi1303 – 1312Combined sources10
Helixi1317 – 1320Combined sources4
Helixi1321 – 1323Combined sources3
Helixi1328 – 1333Combined sources6
Helixi1334 – 1336Combined sources3
Helixi1338 – 1347Combined sources10
Turni1348 – 1350Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8BNMR-A1271-1351[»]
ProteinModelPortaliP35187.
SMRiP35187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini687 – 864Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST178
Domaini886 – 1035Helicase C-terminalPROSITE-ProRule annotationAdd BLAST150
Domaini1272 – 1351HRDCPROSITE-ProRule annotationAdd BLAST80

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi808 – 811DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi631 – 639Asp/Glu-rich (highly acidic)9

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HRDC domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074520.
HOGENOMiHOG000141897.
InParanoidiP35187.
KOiK10901.
OMAiSASEQCK.
OrthoDBiEOG092C0HS8.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.80. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR022758. Helicase_Sgs1.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF11408. Helicase_Sgs1. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view]
SUPFAMiSSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTKPSHNLR REHKWLKETA TLQEDKDFVF QAIQKHIANK RPKTNSPPTT
60 70 80 90 100
PSKDECGPGT TNFITSIPAS GPTNTATKQH EVMQTLSNDT EWLSYTATSN
110 120 130 140 150
QYADVPMVDI PASTSVVSNP RTPNGSKTHN FNTFRPHMAS SLVENDSSRN
160 170 180 190 200
LGSRNNNKSV IDNSSIGKQL ENDIKLEVIR LQGSLIMALK EQSKLLLQKC
210 220 230 240 250
SIIESTSLSE DAKRLQLSRD IRPQLSNMSI RIDSLEKEII KAKKDGMSKD
260 270 280 290 300
QSKGRSQVSS QDDNIISSIL PSPLEYNTSS RNSNLTSTTA TTVTKALAIT
310 320 330 340 350
GAKQNITNNT GKNSNNDSNN DDLIQVLDDE DDIDCDPPVI LKEGAPHSPA
360 370 380 390 400
FPHLHMTSEE QDELTRRRNM RSREPVNYRI PDRDDPFDYV MGKSLRDDYP
410 420 430 440 450
DVEREEDELT MEAEDDAHSS YMTTRDEEKE ENELLNQSDF DFVVNDDLDP
460 470 480 490 500
TQDTDYHDNM DVSANIQESS QEGDTRSTIT LSQNKNVQVI LSSPTAQSVP
510 520 530 540 550
SNGQNQIGVE HIDLLEDDLE KDAILDDSMS FSFGRQHMPM SHSDLELIDS
560 570 580 590 600
EKENEDFEED NNNNGIEYLS DSDLERFDEE RENRTQVADI QELDNDLKII
610 620 630 640 650
TERKLTGDNE HPPPSWSPKI KREKSSVSQK DEEDDFDDDF SLSDIVSKSN
660 670 680 690 700
LSSKTNGPTY PWSDEVLYRL HEVFKLPGFR PNQLEAVNAT LQGKDVFVLM
710 720 730 740 750
PTGGGKSLCY QLPAVVKSGK THGTTIVISP LISLMQDQVE HLLNKNIKAS
760 770 780 790 800
MFSSRGTAEQ RRQTFNLFIN GLLDLVYISP EMISASEQCK RAISRLYADG
810 820 830 840 850
KLARIVVDEA HCVSNWGHDF RPDYKELKFF KREYPDIPMI ALTATASEQV
860 870 880 890 900
RMDIIHNLEL KEPVFLKQSF NRTNLYYEVN KKTKNTIFEI CDAVKSRFKN
910 920 930 940 950
QTGIIYCHSK KSCEQTSAQM QRNGIKCAYY HAGMEPDERL SVQKAWQADE
960 970 980 990 1000
IQVICATVAF GMGIDKPDVR FVYHFTVPRT LEGYYQETGR AGRDGNYSYC
1010 1020 1030 1040 1050
ITYFSFRDIR TMQTMIQKDK NLDRENKEKH LNKLQQVMAY CDNVTDCRRK
1060 1070 1080 1090 1100
LVLSYFNEDF DSKLCHKNCD NCRNSANVIN EERDVTEPAK KIVKLVESIQ
1110 1120 1130 1140 1150
NERVTIIYCQ DVFKGSRSSK IVQANHDTLE EHGIGKSMQK SEIERIFFHL
1160 1170 1180 1190 1200
ITIRVLQEYS IMNNSGFASS YVKVGPNAKK LLTGKMEIKM QFTISAPNSR
1210 1220 1230 1240 1250
PSTSSSFQAN EDNIPVIAQK STTIGGNVAA NPPRFISAKE HLRSYTYGGS
1260 1270 1280 1290 1300
TMGSSHPITL KNTSDLRSTQ ELNNLRMTYE RLRELSLNLG NRMVPPVGNF
1310 1320 1330 1340 1350
MPDSILKKMA AILPMNDSAF ATLGTVEDKY RRRFKYFKAT IADLSKKRSS
1360 1370 1380 1390 1400
EDHEKYDTIL NDEFVNRAAA SSNGIAQSTG TKSKFFGANL NEAKENEQII
1410 1420 1430 1440
NQIRQSQLPK NTTSSKSGTR SISKSSKKSA NGRRGFRNYR GHYRGRK
Length:1,447
Mass (Da):163,837
Last modified:February 1, 1994 - v1
Checksum:i0DC320B41756A3C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22341 Genomic DNA. Translation: AAB60289.1.
L07870 Genomic DNA. Translation: AAA35167.1.
Z47815 Genomic DNA. Translation: CAA87811.1.
BK006946 Genomic DNA. Translation: DAA10088.1.
PIRiS50918.
RefSeqiNP_013915.1. NM_001182696.1.

Genome annotation databases

EnsemblFungiiYMR190C; YMR190C; YMR190C.
GeneIDi855228.
KEGGisce:YMR190C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22341 Genomic DNA. Translation: AAB60289.1.
L07870 Genomic DNA. Translation: AAA35167.1.
Z47815 Genomic DNA. Translation: CAA87811.1.
BK006946 Genomic DNA. Translation: DAA10088.1.
PIRiS50918.
RefSeqiNP_013915.1. NM_001182696.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8BNMR-A1271-1351[»]
ProteinModelPortaliP35187.
SMRiP35187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35368. 450 interactors.
DIPiDIP-2911N.
IntActiP35187. 12 interactors.
MINTiMINT-442647.

PTM databases

iPTMnetiP35187.

Proteomic databases

MaxQBiP35187.
PRIDEiP35187.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR190C; YMR190C; YMR190C.
GeneIDi855228.
KEGGisce:YMR190C.

Organism-specific databases

EuPathDBiFungiDB:YMR190C.
SGDiS000004802. SGS1.

Phylogenomic databases

GeneTreeiENSGT00550000074520.
HOGENOMiHOG000141897.
InParanoidiP35187.
KOiK10901.
OMAiSASEQCK.
OrthoDBiEOG092C0HS8.

Enzyme and pathway databases

BioCyciYEAST:G3O-32877-MONOMER.
BRENDAi3.6.4.12. 984.
ReactomeiR-SCE-3108214. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

EvolutionaryTraceiP35187.
PROiP35187.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.80. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR022758. Helicase_Sgs1.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF11408. Helicase_Sgs1. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view]
SUPFAMiSSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSGS1_YEAST
AccessioniPrimary (citable) accession number: P35187
Secondary accession number(s): D6W014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.