SWR1_YEAST
ID SWR1_YEAST Reviewed; 1514 AA.
AC Q05471; D6VSW6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
DE AltName: Full=Swi2/Snf2-related 1;
GN Name=SWR1; OrderedLocusNames=YDR334W; ORFNames=D9651.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
RP FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION IN THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [8]
RP FUNCTION.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1, the
RT Swr1 chromatin remodeling complex, and the histone acetyltransferase
RT NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [9]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645854; DOI=10.1126/science.1090701;
RA Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT remodeling complex.";
RL Science 303:343-348(2004).
CC -!- FUNCTION: Catalytic component of the SWR1 complex which mediates the
CC ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading
CC to transcriptional regulation of selected genes by chromatin
CC remodeling. {ECO:0000269|PubMed:14645854, ECO:0000269|PubMed:14690608,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15353583}.
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 -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex composed of
CC at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4,
CC SWC5, SWC7 and SWR1, and perhaps BDF1. {ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC -!- INTERACTION:
CC Q05471; P35817: BDF1; NbExp=3; IntAct=EBI-22102, EBI-3493;
CC Q05471; Q12692: HTZ1; NbExp=9; IntAct=EBI-22102, EBI-8080;
CC Q05471; P53201: SWC4; NbExp=7; IntAct=EBI-22102, EBI-23061;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; U51032; AAB64770.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12176.1; -; Genomic_DNA.
DR PIR; S70099; S70099.
DR RefSeq; NP_010621.1; NM_001180642.1.
DR PDB; 4M6B; X-ray; 1.78 A; C/F=590-639.
DR PDB; 5I9E; X-ray; 2.80 A; E/H=340-410.
DR PDB; 6GEJ; EM; 3.60 A; M=1-1514.
DR PDB; 6GEN; EM; 3.60 A; M=1-1514.
DR PDBsum; 4M6B; -.
DR PDBsum; 5I9E; -.
DR PDBsum; 6GEJ; -.
DR PDBsum; 6GEN; -.
DR AlphaFoldDB; Q05471; -.
DR SMR; Q05471; -.
DR BioGRID; 32391; 658.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR DIP; DIP-2845N; -.
DR IntAct; Q05471; 40.
DR MINT; Q05471; -.
DR STRING; 4932.YDR334W; -.
DR iPTMnet; Q05471; -.
DR MaxQB; Q05471; -.
DR PaxDb; Q05471; -.
DR PRIDE; Q05471; -.
DR TopDownProteomics; Q05471; -.
DR EnsemblFungi; YDR334W_mRNA; YDR334W; YDR334W.
DR GeneID; 851934; -.
DR KEGG; sce:YDR334W; -.
DR SGD; S000002742; SWR1.
DR VEuPathDB; FungiDB:YDR334W; -.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000167340; -.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q05471; -.
DR OMA; RKKWQYM; -.
DR BioCyc; YEAST:G3O-29890-MON; -.
DR PRO; PR:Q05471; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05471; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0043486; P:histone exchange; IMP:SGD.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR DisProt; DP02295; -.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID50223; -.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Chromatin regulator; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1514
FT /note="Helicase SWR1"
FT /id="PRO_0000074375"
FT DOMAIN 339..411
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 708..873
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1247..1400
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 465..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 824..827
FT /note="DEAH box"
FT COMPBIAS 465..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 721..728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT HELIX 353..389
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:4M6B"
SQ SEQUENCE 1514 AA; 174530 MW; 156E3BB5978905C8 CRC64;
MTTSRKSHAK DKKAGGEQDL ADLKFRYDLL TNELFHLREF VSLVDYDPTH FNDSESFQKF
LRETHLSLEE RGEKFTDDVA KKGTNGDLTR RRRNLRTSTV VSSETTNEKK GDIELKLESI
APLVRNKCEE LKYKLSDHSN RKSIVPQKRP IQHLKKREAA KSLKFKSERK ENPLPLHEHI
AEERYDHIAK VEEPSEAFTI KCPSDDSSFE NTSEHYSDNF YFTTSSEEED IKKKRGRKKK
KPRIKLVVHP PKQTITNPLH VVKPGYESLH EYIASFKSLE DDLTLEEYNK YIDEQRRLLS
RLKKGIENGA LKYDKETDSL QPITSKEIKT IITYKPDPIS YFYKQQDLQI HTDHLINQGI
HMSKLFRSST KARIARAKKV SQMIEQHFKH VAGAEERKAK EEERHKKSLA RFAVQAVKKR
WNMAEKAYRI LRKDEEEQLK RIEGKQHLSK MLEKSTQLLE AQLNQVNDDG RSSTPSSDSN
DVLSESDDDM DDELSTSSDE DEEVDADVGL ENSPASTEAT PTDESLNLIQ LKEKYGHFNG
SSTVYDSRNK DEKFPTLDKH ESSSSESSVM TGEESSIYSS SENESQNEND RESDDKTPSV
GLSALFGKGE ESDGDLDLDD SEDFTVNSSS VEGEELEKDQ VDNSAATFER AGDFVHTQNE
NRDDIKDVEE DAETKVQEEQ LSVVDVPVPS LLRGNLRTYQ KQGLNWLASL YNNHTNGILA
DEMGLGKTIQ TISLLAYLAC EKENWGPHLI VVPTSVLLNW EMEFKRFAPG FKVLTYYGSP
QQRKEKRKGW NKPDAFHVCI VSYQLVVQDQ HSFKRKRWQY MVLDEAHNIK NFRSTRWQAL
LNFNTQRRLL LTGTPLQNNL AELWSLLYFL MPQTVIDGKK VSGFADLDAF QQWFGRPVDK
IIETGQNFGQ DKETKKTVAK LHQVLRPYLL RRLKADVEKQ MPAKYEHIVY CKLSKRQRFL
YDDFMSRAQT KATLASGNFM SIVNCLMQLR KVCNHPNLFE VRPILTSFVL EHCVASDYKD
VERTLLKLFK KNNQVNRVDL DFLNLVFTLN DKDLTSYHAE EISKLTCVKN FVEEVNKLRE
TNKQLQEEFG EASFLNFQDA NQYFKYSNKQ KLEGTVDMLN FLKMVNKLRC DRRPIFGKNL
IDLLTKDRRV KYDKSSIIDN ELIKPLQTRV LDNRKIIDTF AVLTPSAVSL DMRKLALGLN
DDSSVGENTR LKVMQNCFEV SNPLHQLQTK LTIAFPDKSL LQYDCGKLQK LAILLQQLKD
NGHRALIFTQ MTKVLDVLEQ FLNYHGYLYM RLDGATKIED RQILTERFNT DSRITVFILS
SRSGGLGINL TGADTVIFYD SDWNPAMDKQ CQDRCHRIGQ TRDVHIYRFV SEHTIESNIL
KKANQKRQLD NVVIQEGDFT TDYFSKLSVR DLLGSELPEN ASGGDKPLIA DADVAAKDPR
QLERLLAQAE DEDDVKAANL AMREVEIDND DFDESTEKKA ANEEEENHAE LDEYEGTAHV
DEYMIRFIAN GYYY
