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Database: UniProt
Entry: Q6CA87
LinkDB: Q6CA87
Original site: Q6CA87 
ID   SWR1_YARLI              Reviewed;        1772 AA.
AC   Q6CA87;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   31-JUL-2019, entry version 101.
DE   RecName: Full=Helicase SWR1;
DE            EC=3.6.4.12;
GN   Name=SWR1; OrderedLocusNames=YALI0D04961g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(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. {ECO:0000250}.
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.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00549}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR382130; CAG80613.1; -; Genomic_DNA.
DR   RefSeq; XP_502425.1; XM_502425.1.
DR   SMR; Q6CA87; -.
DR   PRIDE; Q6CA87; -.
DR   EnsemblFungi; CAG80613; CAG80613; YALI0_D04961g.
DR   GeneID; 2910662; -.
DR   KEGG; yli:YALI0D04961g; -.
DR   HOGENOM; HOG000186095; -.
DR   InParanoid; Q6CA87; -.
DR   KO; K11681; -.
DR   OMA; NKPDAFH; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
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:0043044; P:ATP-dependent chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0016458; P:gene silencing; IBA:GO_Central.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00573; HSA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Chromatin regulator; Complete proteome;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1   1772       Helicase SWR1.
FT                                /FTId=PRO_0000074374.
FT   DOMAIN      536    609       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      921   1086       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1470   1623       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     934    941       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF      1037   1040       DEAH box.
FT   COMPBIAS    125    868       Glu-rich.
SQ   SEQUENCE   1772 AA;  202404 MW;  9D9C8787FF55D07A CRC64;
     MSKRTQDLAT THANGSVDSA TAPGASKRRR LADPVLDTPV ELLASGRRTS GRHRPVEDAS
     RQATQQQQAP GTPGGRQQRR AAAAAKESLS TPKRAPAKPK EKTPKATPKK TPSRRNGRRR
     SVKVEEVEEE EPEEEEGPEE EEAPEEEVEG DDEEEVQVEE EAEPVSLTPL EEKKQELAKL
     ISDNDSRVRL LFHLKQFVSL VFYDPAEAKQ DQSSVWEQVS MRESIIGTRT RLTQFQQNYD
     LWTKYLERKT GGHMRSTRRQ IRSKQGALED DFVIKLKEEM TAVEEEEEEE LVEEEEEEEE
     EEEQEEDEEQ EQQEEEEEEQ EEEVTSRRGS RRSAPTKAKG KSKTASKTSK SKSKASSKSK
     SKSKGKGQAR ASKLSKSRRY VNAVDSSSEE ESDYDPNKPY DVSKEVWEPI DTGWLLPDSE
     DEYYHFDDKF AQHMFPNGVK LKLNVSLKPP RVTHPAHLLL DVAEGQTPDN RERLEGFMSS
     FKLLDEEMTL EEYEEHYERE LETLDKINEM KREGVLQGLA DEEEGESLTV AEIRRGFNDP
     ERSTRPTHWD HVVAQACHFA KLMADERKAH VSQAKRLAAA VDQHFRRLEG AEERDKKAQA
     KLLKTMARKM AQDVMRRWKL AEKVVLKKKE QEAKEEERKQ GKKKLKEILE NSAQLLEARV
     RGDNDTPETE EGEKEEVEAV SDDAMSDVDM EDDREQVEVD TRDDDELTVE ELRAKYAALD
     NIKVERAEEE DEEDEENGDD EDEDEEEDDA EIEEETETTT PALETPIDTP AEEDEFSSDT
     DITLDSEDES SSEQESDYEA ETTAPGLAAL MGGPKAIEED EEEDDAFVIK EEEEEVEVED
     DEEEEKADTE VDRKVETVSE AVGEAVEEIK SNGVESKPTS NGVDVTELDR VTPERAPAVE
     PPFLLRGTLR AYQQLGLEWL AGLYNNDTNG ILADEMGLGK TIQTISLLSY LACEHHIWGP
     HLIIVPTSVM LNWEMEFKRF APGFKVMTYY GNPVQRREKR RGWNKEDTWH VCITSYQLVL
     QDLFAFRRKR WHYMILDEAH NIKNFRSQRW QSLLHFNTVR RLLLTGTPLQ NNLMELWSLL
     YFLMPSSRNQ MDMPGFANLK DFQEWFSRPI DKMVEGGVDE EAKTTVSKLH QILRPYLLRR
     LKKDVEKQMP AKYEHVVYCR LSKRQRYLYD DFMSRAQTRE TLKTGNFLSI INCLMQLRKV
     CNHPDLFEVR PIVTSFVQEQ SVITPYERVS DRVKSLLVNT VDGGYAPSEV SLSFLGFNAE
     LEDMSTHEAT SFRKYHNVQT VKNRIRELEK FCPAETPEEE RYNDIEGHYK HMHHASFQQV
     IGSLKRVEYL HQIALAKKPV YGRNLVEVCT INTSRLQPDR PEETNESSYH WQLTHLRHPT
     VQECANNMAP YIERFACITP KAVTLNMAEL SLGGIGPILQ QRYFKQVTPK KSQRVVVGPP
     AAIADPFHQA QVKLSIAFPD KRLLQYDCGK LQRLATLLQD LIAGGHRALI FTQMTKVLDV
     LEQFLNIHGL RYMRLDGATK IEQRQLLTER FNTDPKIPVF ILSTRSGGLG INLTGADTVI
     FYDSDWNPSM DKQCQDRCHR IGQTRDVHIY RFVSEHTIES NILKKANQKQ ILDNVVIQDG
     EFTTDYFNKM SVHDMLGLEP DDDAAPVADT LNLSGKNLER ALAQAEDADD AAAAKVATKE
     TNLDVEDFDE TQKENNKGAT PGSRSTSATP MEKENTGELS SAMDSPTPVA TPDVAVDNGG
     GDDDDSDSDE SDSGIGHIDE YMIKFIEDGW FW
//
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