SWR1_CANGA
ID SWR1_CANGA Reviewed; 1450 AA.
AC Q6FK48;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; OrderedLocusNames=CAGL0M01188g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62372.1; -; Genomic_DNA.
DR RefSeq; XP_449396.1; XM_449396.1.
DR AlphaFoldDB; Q6FK48; -.
DR SMR; Q6FK48; -.
DR STRING; 5478.XP_449396.1; -.
DR PRIDE; Q6FK48; -.
DR EnsemblFungi; CAG62372; CAG62372; CAGL0M01188g.
DR GeneID; 2891166; -.
DR KEGG; cgr:CAGL0M01188g; -.
DR CGD; CAL0137511; CAGL0M01188g.
DR VEuPathDB; FungiDB:CAGL0M01188g; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q6FK48; -.
DR OMA; RKKWQYM; -.
DR Proteomes; UP000002428; Chromosome M.
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..1450
FT /note="Helicase SWR1"
FT /id="PRO_0000074365"
FT DOMAIN 344..417
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 640..805
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1179..1332
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 469..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 756..759
FT /note="DEAH box"
FT COMPBIAS 516..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 653..700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1450 AA; 167290 MW; 120C95082280BBED CRC64;
MSKNNKLNGK DNRQSKIEKL SELKLRHDQL TNELYHLHEY ISLVEYDPFY IPNSENYERL
LEEKDVTWGS IFQEKKQLHN ESSGKKVRRS VRHLRDSGSS TINELDTMSE NDINLLKEVD
ILAKQKLQDL KLQFSNSHIK KKGNTKRAKI VKQVPNHQDK SESPQISERD VKTVVKDLKP
NHRGSEIKPE IMESSDVKNE IENCDFNEKQ LKLYKDDDIA SESDFYFTTS SEDELPNKRR
GTIKRRKRIN LYVNPPKAVI TNPDNIANSH YPTLHEYLDS FKILEDDMTN EEYNTFIKEQ
QRFAKMIKKG IETGALKYDP VTETVQPSAR KVPNMFSHAK VDPIQYMYKE QNLHIHQEHL
INQGLFSSKL VQNRKKQRIA GAKKIAQMIE QHFKHIAGAE DRRLKENEKQ RKAIARNIIQ
SVKKRWNLAE KAYRILKKDE EEQLKRIQGK EHLSKMLEKS SKLLGAQLKQ HPNEDDIENS
TSDDFSSTGD SDNLSSSSDE ESDDEINDLS EDQKNNINEL KTSSTSAFSS PEISSPSKNP
DLGLNSLLTN DFENESNSSD TNEEFIMGDS DTSHSDDENL TDDSEDSNDG EHDTTSDNEK
SDLFPADTTN DPLAVQDVPT PSLLRGTLRT YQKQGLNWLA SLYNNNTNGI LADEMGLGKT
IQTISLLSYL ACEKHNWGPH LIVVPTSVLL NWEMEFKRFA PGFKVLTYYG NPQQRKEKRK
GWNKPDAFHV CIVSYQLIVQ DQHSFKRKKW QYMVLDEAHN IKNFRSTRWQ ALLNFNTQRR
ILLTGTPLQN NIAELWSLLY FLMPQTVIDG QKVSGFADLD AFQQWFGRPV DKLIETGGTY
EQDNETKRTV EKLHQVLRPY LLRRLKADVE KQIPGKYEHI VYCKLSKRQR FLYDDFMSRA
QTKATLASGN FMSIVNCLMQ LRKVCNHPDL FEVRPIKTSF LFGESVIARY SERANSITRR
IHFHDKDTLV DLQNINLQFT NNDLEKTSYH TNTINKLACI NEFVEEVQKL RKQNAEEERQ
KSRHLKINTQ NISNFYEEFM QQKLDEQENK INFIGYLNSQ RCSRKTVYGM NLIRLLEMPH
VSNNCIDDPN YDDLIKPLQT RLLDGRTTIE KFAVLTPGAV TSNIGELTLG MDEFVTPNSK
SGIIPYEELV QLDNPFHQVQ TKLTIAFPDK SLLQYDCGKL QKLAILLQQL KDGGHRALIF
TQMTKVLDIL EQFLNYHGYL YMRLDGATKI EDRQILTERF NSDPKITVFI LSSRSGGLGI
NLTGADTVIF YDSDWNPAMD KQCQDRCHRI GQTRDVHIYR FVSEHTIESN ILKKANQKRQ
LDDVIIQKGE FTTDYFSKLS VKDLFGSDVV GDLPVIDTKP LLGSDSEAIK DPKKLEKLLA
QAEDEDDVKA ANSALREVNV DDEDFDESST NKTGGNILNG DDIDEDVDEY EGTNHVEEYM
LRFIANGFYF
