SWR1_CRYNB
ID SWR1_CRYNB Reviewed; 1246 AA.
AC P0CO19; Q55LY7; Q5K8T2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; OrderedLocusNames=CNBI2250;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAEY01000044; EAL18964.1; -; Genomic_DNA.
DR RefSeq; XP_773611.1; XM_768518.1.
DR AlphaFoldDB; P0CO19; -.
DR SMR; P0CO19; -.
DR EnsemblFungi; AAW46488; AAW46488; CNL04590.
DR EnsemblFungi; EAL18964; EAL18964; CNBI2250.
DR GeneID; 4938185; -.
DR KEGG; cnb:CNBI2250; -.
DR VEuPathDB; FungiDB:CNBI2250; -.
DR HOGENOM; CLU_000315_24_1_1; -.
DR Proteomes; UP000001435; Chromosome 9.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 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.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Transcription;
KW Transcription regulation.
FT CHAIN 1..1246
FT /note="Helicase SWR1"
FT /id="PRO_0000410114"
FT DOMAIN 405..570
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 939..1092
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 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 521..524
FT /note="DEAH box"
FT COMPBIAS 24..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..365
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418..425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1246 AA; 141185 MW; A28FCC0BFDD2CD07 CRC64;
MSEHNQDLRF LISDDVLNED PMSTGRFAEE DRGSSDTEQL TDNKNDGEEP KETAVQAAFD
GSDDVNRLEE PHNPVSSTAN IGNFALLESS SAEVSDASCP ATMPILVRQS PKTCSQPRTR
KVKLSTLSLS SDPDPDINDP EFKARLEDSN QDDQDEELDL EMEEADSAGR ESGEGNRDSE
DEGLLADADL PIEVLLRRYG YPVPEGEGAV NGEPEQSESK GREQAAPTST VSETLPSTKL
SLAQPANQTD QSLTDTALPE PRVPEQLIIS GKRQRRKKEI WTPDDSEPQH LVGKKRIKKV
EIVEKVEADV HQNGDGLVIV EEETMGDEDN DDSKVGQEEE DGHEYDSEEE YDEDEDEEEE
GAKEDNVDWD DRQDKEGDIG PRVRQPFLLR GTLRPYQQAG LEWLASLWSN NMNGILADEM
GLGKTIQTIA LLGHLACDKG VWGQHLIIVP TSVILNWEME FKKFLPGMKV LTYYGNQKER
KEKRVGWHTE NTWQVCITSY QIVLADQHIF RRKNWCYMIL DEAHNIKNFR SQRWQTLLGF
KAQRRLLLTG TPLQNNLMEL WSLLYFLMPG GIGADATAVV GFANHKEFME WFSNPMDKAI
ETGDAMDEET LETVAKLHTL LRPFILRRLK SEVETQLPGK FEHVVYCRLS KRQRFLYDEF
MSRASTHEAL TTGGYLGVMN TLMQLRKVCN HPDLFEMRPV KTSFAMDNVA RDFEPSDILI
RKRLLAEEDE RRIDALAIGF GVAHNEAMSG WVARARQTYD ASDKLPYAAS PLRRGKLSAP
PPKDTRSVEL WLKYRVWAEE EFSKRRWESI RATNRQRCGI SPIYGSTFLS LLGNLPNFLL
PQDVQSRREE TFADFTPPAA KFITSLPERA KSLEDVIDRF AVIPPNAVAR NLATYALPGL
EPISHPALTD PAFDTLHRSS VKLQIAFPDA SLLQYDCGKL QKLFEMLRDL KSEGHRVLIF
TQMTRVLDIL EMFLSHNGHR YLRLDGSTKI EDRQVLTERF NSDSRIFVFI ASSRSGGVGI
NLTGADTVFF YDSDWNPSMD RQCMDRAHRI GQTREVHIYR FVSSHTVEEN MLRKAEQKRL
LDKMVIQEGG FNNDWWGRVG WKDMFGDVPG ITDVSGVVEK SGEGIIDIQV EGTPVAEDVE
VTRPRAGEER ELARALAEVE DEEDAQAARM AQGEGELDLQ EFEEGPKAVA KRVRVFEPEN
SGTPVTTEAG ETGDVVEEYD DEPGSVEEYM LKWVEEDWDY FSPYRA
