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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //