SWR1_ASHGO
ID SWR1_ASHGO Reviewed; 1486 AA.
AC Q759G7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; OrderedLocusNames=ADR309W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 1066 AND 1341.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52229.2; -; Genomic_DNA.
DR RefSeq; NP_984405.2; NM_209758.2.
DR AlphaFoldDB; Q759G7; -.
DR SMR; Q759G7; -.
DR STRING; 33169.AAS52229; -.
DR PRIDE; Q759G7; -.
DR EnsemblFungi; AAS52229; AAS52229; AGOS_ADR309W.
DR GeneID; 4620571; -.
DR KEGG; ago:AGOS_ADR309W; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q759G7; -.
DR OMA; RKKWQYM; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:0005198; F:structural molecule activity; IEA:EnsemblFungi.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
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..1486
FT /note="Helicase SWR1"
FT /id="PRO_0000074362"
FT DOMAIN 321..393
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 683..848
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1221..1371
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 799..802
FT /note="DEAH box"
FT COMPBIAS 73..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 696..703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1486 AA; 171008 MW; E86FD04A55658AC8 CRC64;
MTKANGAEQL ADWKFQYDLL TNELFHLHEF TSLLEFDPAF RHESDSFARF LADKHLELRM
EEDAGAPGLE ESSAMRRIRR RQKRGRGEEE GNALLKGVEE LVEQKYADLR ARLDRPMLKQ
GPRKRKQPGD AAKTALPHDS KKRKSAVVRK ETNDEEHLKE EKSASPTVWS PESPQRDTYR
TIHPSGDHEG YQSSSSDSFY FTTSSEDEEP TVKRSLKRKK APVRRIKLIV HPPKQTVTNP
LHILKPECSS LHEFLQSYKS LDEDISIEEF DSYIASQRKV VSAIRKGLKS GVLTYDRHTD
SIQGISLKDV QNSQANKPEP ITTFYQEQEK HTLRDHLNNH GVVMSRMFQD RKRGRIARAR
KISQMIEQHF KHVAGAEERK TKEEEKRRRA LARAAVQAVK KRWNLAERAY KVLKKDEEDQ
LKRIQGKEHL SKMLEQSTQL LGAQLNQNDD SDDETSSQVL SENESSLGDE EMSSSSELDD
SEVEAGEDDS KLTVEQLRAK YSALEHITID GRSQNSEVSS MTENPEEDPQ EYKILLSERE
KAELHRTFET EENNILDEDH SSSSSFSESE ISQTSSSENE SLINSNSSQT PGLASLFGNV
AEELSDDAHY STEESLSSTP NEDQEGVQPN ADAVSNMEID SLEMQDKDES TNLEKLSVVD
VPVPPLLRGT LRTYQKQGLN WLASLYNNNT NGILADEMGL GKTIQTIALL AYLACEKENW
GPHLIIVPTS VLLNWEMEFK RFAPGFKVLS YYGSPQQRKE KRRGWNKLDA FHVCITSYQL
VVHDQHSFKR KKWQYMILDE AHNIKNFKST RWQALLNFNT RRRLLLTGTP LQNNIAELWS
LLYFLMPQTA LENGKISGFA DLDAFQQWFG KPVDKIIAAN DSEHDDETRR TVSKLHQVLR
PYLLRRLKAD VEKQMPAKYE HILYCRLSKR QRFLYDDFMS RAQTKATLAS GNFMSIINCL
MQLRKVCNHP DLFEVRPILT SFCMDRSVMS NYAHLNQLVL KNLNKHALDT VVNLQCTNLA
FTQNDFNMET HYADSCARLQ CVRQFSEAVE KLRKDASLPD AKDDPNVLNY QDMHEFYTGY
TVRKRLRLID QYRHTFYLNS LRCEKRPVYG INLVRLVSVH HRPPLECNVM SELMKPLETR
LVTHKRIIDE FAIITPTAIT LDTRVLSLGL DSEAAVHPVI KSDINTQLSR MKNPFHLLQT
KLSIAFPDKS LLQYDCGKLQ SLAVLLRRLK EEGHRALIFT QMTKVLDILE QFLNYHGYLY
MRLDGATKIE DRQILTERFN TDPRITVFIL SSRSGGLGIN LTGADTVIFY DSDWNPAMDK
QCQDRCHRIG QTRDVHIYRF VSEHTIESNI LKKANQKRQL DNIVIQKGEF TTDYFSRLSV
KDLLGSDETE EIADERPLLE DPATTADSKK LERLLAQAED EDDVKAARLA MKEVDVDDRD
FRESSTCANP SPDEDVDEEP VEDEYEGTRH VEEYMIRFIA NGYLYD
