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 14-MAY-2014, entry version 128. 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; OC Saccharomycetes; 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., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] 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., RA Haw R.A., Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., RA Emili A., Hughes T.R., Buratowski S., Greenblatt J.F.; RT "A Snf2 family ATPase complex required for recruitment of the histone RT H2A variant Htz1."; RL Mol. Cell 12:1565-1576(2003). RN [4] 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 [5] 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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] 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 RT Swr1p deposits histone variant H2A.Z into euchromatin."; RL PLoS Biol. 2:587-599(2004). RN [7] 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, RT the Swr1 chromatin remodeling complex, and the histone RT acetyltransferase NuA4."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004). RN [8] 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 RT chromatin remodeling complex."; RL Science 303:343-348(2004). CC -!- FUNCTION: Catalytic component of the SWR1 complex which mediates CC the ATP-dependent exchange of histone H2A for the H2A variant HZT1 CC leading to transcriptional regulation of selected genes by CC chromatin remodeling. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex CC composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, CC VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. CC -!- INTERACTION: CC P60010:ACT1; NbExp=12; IntAct=EBI-22102, EBI-2169; CC P35817:BDF1; NbExp=3; IntAct=EBI-22102, EBI-3493; CC P02293:HTB1; NbExp=2; IntAct=EBI-22102, EBI-8088; CC Q12692:HTZ1; NbExp=8; IntAct=EBI-22102, EBI-8080; CC P53201:SWC4; NbExp=6; IntAct=EBI-22102, EBI-23061; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 CC subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC -!- SIMILARITY: Contains 1 HSA domain. 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 PDBsum; 4M6B; -. DR ProteinModelPortal; Q05471; -. DR SMR; Q05471; 646-1413. DR BioGrid; 32391; 401. DR DIP; DIP-2845N; -. DR IntAct; Q05471; 40. DR MINT; MINT-1165514; -. DR STRING; 4932.YDR334W; -. DR MaxQB; Q05471; -. DR PaxDb; Q05471; -. DR EnsemblFungi; YDR334W; YDR334W; YDR334W. DR GeneID; 851934; -. DR KEGG; sce:YDR334W; -. DR CYGD; YDR334w; -. DR SGD; S000002742; SWR1. DR eggNOG; COG0553; -. DR GeneTree; ENSGT00530000063427; -. DR HOGENOM; HOG000186095; -. DR KO; K11681; -. DR OMA; YMLRFIA; -. DR OrthoDB; EOG77T1D0; -. DR BioCyc; YEAST:G3O-29890-MONOMER; -. DR NextBio; 970001; -. DR Genevestigator; Q05471; -. 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. 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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR014012; Helicase/SANT-assoc_DNA-bd. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF07529; HSA; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 3. 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; KW Complete proteome; DNA-binding; Helicase; Hydrolase; KW Nucleotide-binding; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 1514 Helicase SWR1. FT /FTId=PRO_0000074375. FT DOMAIN 339 411 HSA. FT DOMAIN 708 873 Helicase ATP-binding. FT DOMAIN 1247 1400 Helicase C-terminal. FT NP_BIND 721 728 ATP (Potential). FT MOTIF 824 827 DEAH box. FT HELIX 602 605 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 //