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Database: UniProt
Entry: Q6BKC2
LinkDB: Q6BKC2
Original site: Q6BKC2 
ID   SWR1_DEBHA              Reviewed;        1616 AA.
AC   Q6BKC2; B5RUM2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   31-JUL-2019, entry version 97.
DE   RecName: Full=Helicase SWR1;
DE            EC=3.6.4.12;
GN   Name=SWR1; OrderedLocusNames=DEHA2F23188g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAR66400.1; -; Genomic_DNA.
DR   RefSeq; XP_002770883.1; XM_002770837.1.
DR   SMR; Q6BKC2; -.
DR   STRING; 4959.XP_002770883.1; -.
DR   PRIDE; Q6BKC2; -.
DR   EnsemblFungi; CAR66400; CAR66400; DEHA2F23188g.
DR   GeneID; 8999049; -.
DR   KEGG; dha:DEHA2F23188g; -.
DR   HOGENOM; HOG000186095; -.
DR   InParanoid; Q6BKC2; -.
DR   KO; K11681; -.
DR   OMA; NKPDAFH; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005198; F:structural molecule activity; IEA:EnsemblFungi.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.10810; -; 1.
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   SUPFAM; SSF52540; SSF52540; 2.
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   1616       Helicase SWR1.
FT                                /FTId=PRO_0000074367.
FT   DOMAIN      396    468       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      793    958       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1333   1486       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     806    813       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       909    912       DEAH box.
SQ   SEQUENCE   1616 AA;  184664 MW;  096466AA99278784 CRC64;
     MARGGSRRRN TSVISTQKIE PSNESTKAPE GPQKRKPKTE IPNSNGNGVI KKEIKKRKLD
     NELDESQEHL AQLITDFNLS VNELFQLKEY KTIAYWNPDD FSRASSTSQV PEIFDLFSKE
     PEYQISWGAD SNEQDLSNIP LRLQKKIINE REQKLLEKFP FKEKVLKRSR DLEIELLQNI
     RQSKKTLEKS HIKPSPPVKP SKTSKGNQKI IKKKQVVKQE EEEAQENHQN EEYESDMDEG
     THYKLKAVKY SIPPPIVTHP SHIPSWVPDP NHTESSFNSK DSEIIDYHPD AIQFVSNSKT
     TYTTPNIQAK IQNFLASYKS AIIDETSSGD FNNTLEEYEK IMTQQEQFIK KLYEKTSIEK
     RLELNGEKIE RRKTVLPHSS NTKQAVDPFR SHGAIIPKTQ GVTIHSTHHD YFLSHGMAFS
     RLHQQMRRQH QLRTKKITQM IEQHFKKKKG EKERLAKEKE QNLKRISKMA VQAVKKRWIQ
     ASKVYRFLQL QKEEELKKIK GREHLSQMLE HSTQLLEAQF NKSSRDISEV DTENENETDD
     HLSSSSDEDS GSPQNARDDS NVNMDENDMQ LTVEELRAKY ADIDQSIEPS SKTISSDSSN
     HESDSDDEDI DANKGLVALY GNNAVSVEPV SSLAATEYTD EQKTLIEKFS KEDEGISSES
     VSDDSLNDSS SSESDDDSEV DESNHKQVDS TKPTGLAALL GNGPTEDEED SNDDVSADSD
     GNVSDDENMS TTDEEDEPKT PKSSEDPKMD EKENESDVLE EEVNGSKVRD VPLPPLLRGT
     LRPYQKQGLN WLASLYNNGT NGILADEMGL GKTIQTISLL AYLAAEHHIW GPHLIVVPTS
     VMLNWEMEFK KFAPGFKVLT YYGSPQQRAQ KRKGWNKPNA FHVCITSYQL VVHDHQSFKR
     RRWRYMILDE AHNIKNFRSA RWRALLNFNT ENRLLLTGTP LQNNLMELWS LLYFLMPSSK
     VNQAMPDGFA NLEDFQTWFG RPVDKILEKT SNGTSSDVID ENDKTTQRMD EETRNTVSRL
     HQVLRPYLLR RLKKDVEKQM PGKYEHIIYC RLSKRQRYLY DDFMSRAQTK ETLASGNFLS
     IINCLMQLRK VCNHPDLFEV RPIVTSLAMP RCVANSFAST DSVVRKYLND DSFKGQVSLK
     ALNLDITSLD QLNYFTSQTT SKLKSSSELD KQADKLNELI SASEYDQPNL DNFLEYYKFI
     KSNEQVGIRD NLKHASYLNS LRCDRIPLLG ESVIKFLQTA TQPRQPFTDA YNDIILSIPK
     RVEKMDDVIE KYSVLTPSVV TLDLKDQLIP LSTQRTIMNE VANKNIDNPF HKSQVKLSIA
     FPDKSLLQFD CGKLQKLATL LQDLTANGHR ALIFTQMTKV LDILEQFLNI HGYRYMRLDG
     ATKIEDRQLL TEKFNRDSKI PVFILSTRSG GLGINLTGAD TVIFYDSDWN PAMDKQCQDR
     CHRIGQSRDV HIYRFVSEYT IESNILRKAN QKRQLDNVVI QEGEFTTDYF GKFSVKDLVN
     DAEVADIPDK PLEPAYGNVE NVLAQAEDED DRVAANAAMK EVAIDDEDFD EESKAATNTA
     TPSQTPGPDT AGSGIVDSTV KINNKTDSLE DVDYEDGVSH VDEYMLRFIA NGYYWD
//
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