Q05471 (SWR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Helicase SWR1
EC=3.6.4.12

Alternative name(s):
Swi2/Snf2-related 1

Gene names

Name:	SWR1
Ordered Locus Names:	YDR334W
ORF Names:	D9651.6

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1514 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Ref.3 Ref.6 Ref.7 Ref.8
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Component of the SWR1 chromatin-remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1.
Subcellular location	Nucleus Ref.4.
Miscellaneous	Present with 656 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator Chromatin regulator Helicase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histone exchange Inferred from mutant phenotype Ref.8. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Swr1 complex Inferred from direct assay Ref.8Ref.3. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW helicase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.8. Source: IntAct structural molecule activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACT1	P60010	5	EBI-22102,EBI-2169
BDF1	P35817	3	EBI-22102,EBI-3493
HTB1	P02293	2	EBI-22102,EBI-8088
HTZ1	Q12692	8	EBI-22102,EBI-8080
SWC4	P53201	6	EBI-22102,EBI-23061

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1514	1514	Helicase SWR1		PRO_0000074375
Regions
	Domain	339 – 411	73	HSA
	Domain	708 – 873	166	Helicase ATP-binding
	Domain	1247 – 1400	154	Helicase C-terminal
	Nucleotide binding	721 – 728	8	ATP Potential
	Motif	824 – 827	4	DEAH box

Sequences

	Sequence		Length	Mass (Da)
	Q05471 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 156E3BB5978905C8	FASTA	1,514	174,530
	10 20 30 40 50 60 MTTSRKSHAK DKKAGGEQDL ADLKFRYDLL TNELFHLREF VSLVDYDPTH FNDSESFQKF 70 80 90 100 110 120 LRETHLSLEE RGEKFTDDVA KKGTNGDLTR RRRNLRTSTV VSSETTNEKK GDIELKLESI 130 140 150 160 170 180 APLVRNKCEE LKYKLSDHSN RKSIVPQKRP IQHLKKREAA KSLKFKSERK ENPLPLHEHI 190 200 210 220 230 240 AEERYDHIAK VEEPSEAFTI KCPSDDSSFE NTSEHYSDNF YFTTSSEEED IKKKRGRKKK 250 260 270 280 290 300 KPRIKLVVHP PKQTITNPLH VVKPGYESLH EYIASFKSLE DDLTLEEYNK YIDEQRRLLS 310 320 330 340 350 360 RLKKGIENGA LKYDKETDSL QPITSKEIKT IITYKPDPIS YFYKQQDLQI HTDHLINQGI 370 380 390 400 410 420 HMSKLFRSST KARIARAKKV SQMIEQHFKH VAGAEERKAK EEERHKKSLA RFAVQAVKKR 430 440 450 460 470 480 WNMAEKAYRI LRKDEEEQLK RIEGKQHLSK MLEKSTQLLE AQLNQVNDDG RSSTPSSDSN 490 500 510 520 530 540 DVLSESDDDM DDELSTSSDE DEEVDADVGL ENSPASTEAT PTDESLNLIQ LKEKYGHFNG 550 560 570 580 590 600 SSTVYDSRNK DEKFPTLDKH ESSSSESSVM TGEESSIYSS SENESQNEND RESDDKTPSV 610 620 630 640 650 660 GLSALFGKGE ESDGDLDLDD SEDFTVNSSS VEGEELEKDQ VDNSAATFER AGDFVHTQNE 670 680 690 700 710 720 NRDDIKDVEE DAETKVQEEQ LSVVDVPVPS LLRGNLRTYQ KQGLNWLASL YNNHTNGILA 730 740 750 760 770 780 DEMGLGKTIQ TISLLAYLAC EKENWGPHLI VVPTSVLLNW EMEFKRFAPG FKVLTYYGSP 790 800 810 820 830 840 QQRKEKRKGW NKPDAFHVCI VSYQLVVQDQ HSFKRKRWQY MVLDEAHNIK NFRSTRWQAL 850 860 870 880 890 900 LNFNTQRRLL LTGTPLQNNL AELWSLLYFL MPQTVIDGKK VSGFADLDAF QQWFGRPVDK 910 920 930 940 950 960 IIETGQNFGQ DKETKKTVAK LHQVLRPYLL RRLKADVEKQ MPAKYEHIVY CKLSKRQRFL 970 980 990 1000 1010 1020 YDDFMSRAQT KATLASGNFM SIVNCLMQLR KVCNHPNLFE VRPILTSFVL EHCVASDYKD 1030 1040 1050 1060 1070 1080 VERTLLKLFK KNNQVNRVDL DFLNLVFTLN DKDLTSYHAE EISKLTCVKN FVEEVNKLRE 1090 1100 1110 1120 1130 1140 TNKQLQEEFG EASFLNFQDA NQYFKYSNKQ KLEGTVDMLN FLKMVNKLRC DRRPIFGKNL 1150 1160 1170 1180 1190 1200 IDLLTKDRRV KYDKSSIIDN ELIKPLQTRV LDNRKIIDTF AVLTPSAVSL DMRKLALGLN 1210 1220 1230 1240 1250 1260 DDSSVGENTR LKVMQNCFEV SNPLHQLQTK LTIAFPDKSL LQYDCGKLQK LAILLQQLKD 1270 1280 1290 1300 1310 1320 NGHRALIFTQ MTKVLDVLEQ FLNYHGYLYM RLDGATKIED RQILTERFNT DSRITVFILS 1330 1340 1350 1360 1370 1380 SRSGGLGINL TGADTVIFYD SDWNPAMDKQ CQDRCHRIGQ TRDVHIYRFV SEHTIESNIL 1390 1400 1410 1420 1430 1440 KKANQKRQLD NVVIQEGDFT TDYFSKLSVR DLLGSELPEN ASGGDKPLIA DADVAAKDPR 1450 1460 1470 1480 1490 1500 QLERLLAQAE DEDDVKAANL AMREVEIDND DFDESTEKKA ANEEEENHAE LDEYEGTAHV 1510 DEYMIRFIAN GYYY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1." Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A., Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A., Hughes T.R., Buratowski S., Greenblatt J.F. Mol. Cell 12:1565-1576(2003) [PubMed: 14690608] [Abstract] Cited for: FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION IN THE SWR1 COMPLEX, MASS SPECTROMETRY.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin." Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J. PLoS Biol. 2:587-599(2004) [PubMed: 15045029] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, MASS SPECTROMETRY.
[7]	"Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4." Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F. Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed: 15353583] [Abstract] Cited for: FUNCTION.
[8]	"ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex." Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C. Science 303:343-348(2004) [PubMed: 14645854] [Abstract] Cited for: IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51032 Genomic DNA. Translation: AAB64770.1. BK006938 Genomic DNA. Translation: DAA12176.1.
PIR	S70099.
RefSeq	NP_010621.1. NM_001180642.1.
3D structure databases
ProteinModelPortal	Q05471.
SMR	Q05471. Positions 686-1398.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2845N.
IntAct	Q05471. 42 interactions.
MINT	MINT-1165514.
STRING	Q05471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR334W; YDR334W; YDR334W.
GeneID	851934.
KEGG	sce:YDR334W.
NMPDR	fig|4932.3.peg.1387.
Organism-specific databases
CYGD	YDR334w.
SGD	S000002742. SWR1.
Phylogenomic databases
eggNOG	fuNOG05537.
GeneTree	EFGT00050000000148.
HOGENOM	HBG396531.
OMA	NWLASLY.
OrthoDB	EOG49S9FK.
Gene expression databases
ArrayExpress	Q05471.
Genevestigator	Q05471.
GermOnline	YDR334W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR014001. DEAD-like_helicase. IPR014012. Helicase/SANT-assoc_DNA-bd. IPR001650. Helicase_C. IPR006562. HSA. IPR000330. SNF2_N. [Graphical view]
KO	K11681.
Pfam	PF00271. Helicase_C. 1 hit. PF07529. HSA. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS00690. DEAH_ATP_HELICASE. False negative. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51204. HSA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970001.

Entry information

Entry name

SWR1_YEAST

Accession

Primary (citable) accession number: Q05471
Secondary accession number(s): D6VSW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program