SWR1_DEBHA
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 03-AUG-2022, entry version 107.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; OrderedLocusNames=DEHA2F23188g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAR66400.1; -; Genomic_DNA.
DR RefSeq; XP_002770883.1; XM_002770837.1.
DR AlphaFoldDB; Q6BKC2; -.
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 VEuPathDB; FungiDB:DEHA2F23188g; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q6BKC2; -.
DR OMA; RKKWQYM; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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 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..1616
FT /note="Helicase SWR1"
FT /id="PRO_0000074367"
FT DOMAIN 396..468
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 793..958
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1333..1486
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 909..912
FT /note="DEAH box"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..733
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 806..813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
