SWR1_YARLI
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 03-AUG-2022, entry version 111.
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 lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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., 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; CR382130; CAG80613.1; -; Genomic_DNA.
DR RefSeq; XP_502425.1; XM_502425.1.
DR AlphaFoldDB; Q6CA87; -.
DR SMR; Q6CA87; -.
DR STRING; 4952.CAG80613; -.
DR PRIDE; Q6CA87; -.
DR EnsemblFungi; CAG80613; CAG80613; YALI0_D04961g.
DR GeneID; 2910662; -.
DR KEGG; yli:YALI0D04961g; -.
DR VEuPathDB; FungiDB:YALI0_D04961g; -.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q6CA87; -.
DR OMA; RKKWQYM; -.
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:ATP hydrolysis activity; IBA:GO_Central.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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-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; 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; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1772
FT /note="Helicase SWR1"
FT /id="PRO_0000074374"
FT DOMAIN 536..609
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 921..1086
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1470..1623
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1037..1040
FT /note="DEAH box"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..322
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..373
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..705
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..758
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..796
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..847
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 934..941
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
