SWR1_KLULA
ID SWR1_KLULA Reviewed; 1572 AA.
AC Q6CJ38;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; OrderedLocusNames=KLLA0F21758g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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 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: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-ProRule:PRU00549}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR382126; CAG98759.1; -; Genomic_DNA.
DR RefSeq; XP_456051.1; XM_456051.1.
DR AlphaFoldDB; Q6CJ38; -.
DR SMR; Q6CJ38; -.
DR STRING; 28985.XP_456051.1; -.
DR EnsemblFungi; CAG98759; CAG98759; KLLA0_F21758g.
DR GeneID; 2895412; -.
DR KEGG; kla:KLLA0_F21758g; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q6CJ38; -.
DR OMA; RKKWQYM; -.
DR Proteomes; UP000000598; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0005198; F:structural molecule activity; IEA:EnsemblFungi.
DR GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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-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 3: Inferred from homology;
KW Activator; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1572
FT /note="Helicase SWR1"
FT /id="PRO_0000074370"
FT DOMAIN 424..496
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 777..942
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1314..1464
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 61..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 893..896
FT /note="DEAH box"
FT COMPBIAS 61..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 790..797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1572 AA; 179228 MW; BCD2E07B63FE0211 CRC64;
MPEVRDWRQL AKTRLEYELL TNELFHLWEF TSLVEYDPLF RNTSNSFKTF LQERGLDVES
SLEQDDMKES NASRRLKRRN VISGTADSSS DKNNIWGQVM PLVDQEYSEL QEKLRASVCG
RRGRKRTQQV ASVPAESEED VAVPRPNKKR QTVVTAQGSA QNKLNTPVVS SPKKSLKQTA
DKKSKLNKRD SSTNDISVES EDPPVKDITN TGQGKSKARL KSSKAKSKKR AVKSQTELVR
KQSPEIKNES KRTKADPTHT NDDGNDNRKT NNKSKNIINN NESGLKTSLN TTGDIIDDEE
YYFTSSSEDD DNEKPRTALQ KKSLPNRLKV KLHVNAPRQT ITNPLHVLKP EYADVHSFLQ
SYKSLDEDVS LEEYDSYIKE QRKTAKLIRI GFERGAIKYD PQTDSLQSLS LRDVMPPSNA
AEPISVYYKE QSKHTFQDHL VNQGIVLSKS FQDSRRSQIA KARRVAQIIE SHFKHIAGAE
ERKLKEEEKR KKNLARFAMQ AVKKRWTMAE KAYKVLKKDE LDQLERIQGK QHLTEMLEQS
TQLLGAQLNQ LDSCTYPSEA SDASSEFSAN EESDGNSDID DEMMSTSSCD SDKEGNTERI
GNDMELSVEE LRSKYAQLNK INDFGNETSK SAADESIFDE ASDSVSDSME DSLSSSESET
EDADASAQED TPGLSALLGN IDENEEDVEA DVNFDADSSS DDGLDGDSSG AENNSKTEEL
PSPPKSDNEL KDEKAETTES VTSPAAADPL AVSDVPVPSL LRGTLRIYQK QGLNWLASLY
NNKTNGILAD EMGLGKTIQT ISLLAYLACE KENWGPHLIV VPTSVLLNWE MEFKRFAPGF
KVLTYYGSPQ QRREKRKGWN KPDAFHVCIT SYQLVVHDQH SFKRKKWQYM ILDEAHNIKN
FRSTRWQALL NFNTERRLLL TGTPLQNNLA ELWSLLYFLM PQTALENGKV SGFADLDAFQ
QWFGRPVDKI VETGENYEQD EETKKTVSKL HQVLRPYLLR RLKADVEKQM PGKYEHIIYC
RLSKRQRFLY DDFMSRAQTK ETLASGNFMS IINCLMQLRK VCNHPDLFEV RPILTSFCIE
DSVSKSYCDL NNYVYNRLHE NQFETSVDLS NLNFQFTSND KTLSTNHSEK ISELQCVQPI
LKEISRLKQL NENDSPVTQP DFQDLNQYYS YAKHNKINEI IGQLEHLNYM NNLRCNRRPM
YGSNIVKLLT VGPKKFIDCE LTQESIKPLE TRLLEGKETI EKFAVITPPV VTLDIRERAV
GVDDNNKRFE ESVKHHLVSQ MRSLENPFHQ LQTKLSVAFP DKSLLQYDCG KLQKLAQLLQ
NLKDNGHRAL IFTQMTKVLD ILEQFLNFHG YLYMRLDGAT KIEDRQILTE RFNSDPRITV
FILSSRSGGL GINLTGADTV IFYDSDWNPA MDKQCQDRCH RIGQTRDVHI YRFVSDHTIE
SNILKKANQK RHLDNVVIQT GDFTTDYFTK LSVKDLLGAE APEDIPDDKP LLQDQKNLNK
LLAQAEDEDD AKAAKSALRE VNVDNEDFQE GSVAAQDGNS DNENNEDSED EYGGTSHVEE
YMVRFIANGF YY
