SWR1_CANAL
ID SWR1_CANAL Reviewed; 1641 AA.
AC Q59U81; A0A1D8PHY5; Q59UC7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; OrderedLocusNames=CAALFM_C207560WA;
GN ORFNames=CaO19.1871, CaO19.9427;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017624; AOW27754.1; -; Genomic_DNA.
DR RefSeq; XP_713128.2; XM_708035.2.
DR AlphaFoldDB; Q59U81; -.
DR SMR; Q59U81; -.
DR STRING; 237561.Q59U81; -.
DR PRIDE; Q59U81; -.
DR GeneID; 3645220; -.
DR KEGG; cal:CAALFM_C207560WA; -.
DR CGD; CAL0000190429; SWR1.
DR VEuPathDB; FungiDB:C2_07560W_A; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; Q59U81; -.
DR OrthoDB; 188211at2759; -.
DR PRO; PR:Q59U81; -.
DR Proteomes; UP000000559; Chromosome 2.
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 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; Coiled coil; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1641
FT /note="Helicase SWR1"
FT /id="PRO_0000074364"
FT DOMAIN 416..488
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 835..1000
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1367..1520
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..521
FT /evidence="ECO:0000255"
FT MOTIF 951..954
FT /note="DEAH box"
FT COMPBIAS 9..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 848..855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1641 AA; 187725 MW; 2FB794E82D3F78F4 CRC64;
MPENGRLRRT SARLTQNGTS TSSSTIYQNG KRTSQHAQET STASNKKRKV STQSKEDKLS
DIIVDFNLAV NELYQLKEYK SIISWDPIEN SSANDRGIKA EFEEFVKNND YRLVWDKEIE
NNSNIDSLPL RFQKKKLAEQ NKLLDDKFSI RQNVLASSKM LEESLVNKTR DEVKIESTFK
AIQSQEKAGS KLKTPSQTSN AKTNIRKSGS TTPKRGNENG SRKQALEDQD EIIELSDDSS
VVEIESDLSD AETHYRIKCI KKTVPPPLVT HPSHIPQWRP ENLEDGNRST GRLIQLKDSS
SSSKIINFDP TPLEIIQLKD EVIAAPKLTE KLQNFLNNDF KTPIIDESNV PDYNFTRDEY
NTIMSQQEKL LRKLYHKVNI ENSLELNGDK IERRKVILPQ SNIKLTDPFR NTFSVKPKLH
GAANNATHQD YLLAQGMAFS KVHQQMRKQH HLRTRKIAAM IDQHFKKKKG EKERLAKERE
QNLKKMSRLT MQAVKKRWNQ AQKVYQIIQN EKEEELKKIK GRQHLSEMLE HSTQLLEAQL
TSSREPTVEA ESDDNSTTFD DNTNDSDNFS SSEEEENEED NTQQQINGNK KYDVNGKSND
ENDMSLSVEE LRKKYADLET SVEPLSSNVT SDKERESETS SEDAESSDDD DTDVTRGLAS
LYQNDEVADF ATTTFEYSAE EKKLIEDLNQ ESDSRMNSLL DSDSVSSISD SESSEESSSD
TEMDQSNVSE PPRSSETGSN TGLASLFTNG TIVSDEEDDA SISSNFENES DESMNSSDRE
LEVNGNGKID KIASTDEDDS NVEIVNGSKV KDVPIPSLLR GTLRPYQKQG LNWLASLYNN
NTNGILADEM GLGKTIQTIS LLAYLACEHH KWGPHLIIVP TSVMLNWEME FKKFAPGFKV
LTYYGSPQQR AQKRKGWNKP DAFHVCITSY QLVVQDQQSF KRRRWTYMIL DEAHNIKNFR
STRWRALLNF NTENRLLLTG TPLQNNLMEL WSLLYFLMPS SKVNQAMPEG FANLDDFQQW
FGKPVDRILE QTSAGNSDLI DENERTTQKM DEETRNTVAR LHQVLRPYLL RRLKKDVEKQ
MPGKYEHIVY CRLSKRQRFL YDDFMSRAKT KETLASGNFL SIINCLMQLR KVCNHPDLFE
VRPIVTSFAM PRSIPSYYQS TNELVKRQFN KDEKVSFQAL NLDVTGCENM NYFVCQSTGK
LMTTEPFQDQ INKLKILLVE FENSDPINYV SYYQRLRREE QAEIKEKLEH VVYLNNLRCG
RKPIYGESLL RLLTVNAHDF SDEPYNKYCL TLSGRVDKMN DTIEKYSIIT PAAVALDMKD
QLIPISTKQR ILHEVAENKI DNPFHKAQVK LSIAFPDKTL LQYDCGKLQK LATLLQELTS
QGHRALIFTQ MTKVLDILEQ FLNIHGYRYM RLDGATKIED RQLLTEKFNR DPKIPVFILS
TRSGGLGINL TGADTVIFYD SDWNPAMDKQ CQDRCHRIGQ VRDVHIYRFV SEYTIESNII
KKANQKRQLD NVVIQEGEFT TDYFGKFSVR DLVSDSNIGK EITDRTIDFS GDAKMGNVLA
QAEDEEDRVA AGAALKEVAI DDDDFKEETR SATTGATPAP TETNALSTTD GDAAFIDVDY
EDGIGHIDEY MLRFISDGYY L
