SWR1_SCHPO
ID SWR1_SCHPO Reviewed; 1288 AA.
AC O13682; Q9URL5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Helicase swr1;
DE EC=3.6.4.12;
GN Name=swr1; ORFNames=SPAC11E3.01c, SPAC2H10.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAA22447.1; -; Genomic_DNA.
DR PIR; T37528; T37528.
DR RefSeq; XP_001713118.1; XM_001713066.2.
DR AlphaFoldDB; O13682; -.
DR SMR; O13682; -.
DR BioGRID; 280637; 232.
DR STRING; 4896.SPAC11E3.01c.1; -.
DR iPTMnet; O13682; -.
DR MaxQB; O13682; -.
DR PaxDb; O13682; -.
DR PRIDE; O13682; -.
DR EnsemblFungi; SPAC11E3.01c.1; SPAC11E3.01c.1:pep; SPAC11E3.01c.
DR PomBase; SPAC11E3.01c; swr1.
DR VEuPathDB; FungiDB:SPAC11E3.01c; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; O13682; -.
DR OMA; RKKWQYM; -.
DR PhylomeDB; O13682; -.
DR PRO; PR:O13682; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; NAS:PomBase.
DR GO; GO:0003677; F:DNA binding; IC:PomBase.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
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..1288
FT /note="Helicase swr1"
FT /id="PRO_0000074372"
FT DOMAIN 105..177
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 459..624
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 995..1150
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 275..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 575..578
FT /note="DEAH box"
FT COMPBIAS 281..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1288 AA; 149456 MW; 5524869B79F4A39E CRC64;
MTYEESEKNK NGLSSYIKKE GSSDLKVRVR FREPKLLVTH SGHITEQPKY EHLEQYLDSY
VSLEDGDHDP KEAKELVFRE VQLRHRINEF RKKGYFTAEA PVELKKAPSS NNIPISYRDN
LLSHVNGYAR SMHNDRKVRA SRSRRISGMI LAHFKRLSGA DEKKAKEEDK RIRLLAKRTA
WEIRKKWKVI EREVRRRRAE RAAEAQRVAG KEQLANILKH STDLLEARIE RANINISAQT
SESAVDWNYL LKTSDDLLSV DELKLKYSNP DLIKNIEREE EAEETSDDEP LSSEDEENED
EDITEESNLR KRKVSDKTRV VNKHPPSLRR SRRFFAKKSY NHVSDLDGEV IVMKKEDITD
GVSTKKDLND GDQNEVPLHD TGSSSSLSLL YNEDVASKKK RRVNDDGLAR KKSIAGISEQ
RKFDEPNGSP VLHANKIQVP FLFRGTLREY QQYGLEWLTA LHDSNTNGIL ADEMGLGKTI
QTIALLAHLA CEKENWGPHL IIVPTSVMLN WEMEFKKFLP GFKILTYYGN PQERKEKRSG
WYKPDTWHVC ITSYQLVLQD HQPFRRKKWQ YMILDEAHNI KNFRSQRWQS LLNFNAEHRL
LLTGTPLQNN LVELWSLLYF LMPAGVTQNN SAFANLKDFQ DWFSKPMDRL IEEGQDMNPE
AMNTVAKLHR VLRPYLLRRL KTEVEKQMPA KYEHVVYCQL SKRQRFLYDD FINRARTREI
LASGNFMSII NCLMQLRKVC NHPNLHEERP IVTSFALRRS AIADLEIKDL LVRKRLLHEE
PMTKLDLSTL RLIRTDSEAF DTFVSDELNS LCATNAYNRI STFLRMQIDE ECKPCQFKKS
NFKEHFQNKI YQEQLDKLNF QKYLNESKCS HSPIYGSNLI RLAEKLPKHS TSIDYTLYAK
DDPLYLLNTT KALRSCILST EERASNMKEI IQRFACITPK AVVVDLPELF CKTIPRDLLY
EVSRKINPLH QASTRLAIAF PDKRLLQYDC GKLQVLDRLL KDLVSNGHRV LIFTQMTKVL
DILEQFLNIH GHRYLRLDGA TKIEQRQILT ERFNNDDKIP VFILSTRSGG LGINLTGADT
VIFYDSDWNP QLDAQAQDRS HRIGQTRDVH IYRLISEYTV ESNMLRRANQ KRMLDKIVIQ
GGEFTTEWFR KADVLDLFDL DDESLKKVKA DSDSGSTKNE ENWEVALAAA EDEEDVQAAQ
VARKESALEQ TEFSETSTPQ AMLTKDSTPL SSDSATPGFE RDSTEEQSNT NDMDEDRSEL
EEDLDETVGH IDEYMISFLE QEGTSDEW
