SWR1_ASPFU
ID SWR1_ASPFU Reviewed; 1695 AA.
AC Q4WAS9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Helicase swr1;
DE EC=3.6.4.12;
GN Name=swr1; ORFNames=AFUA_7G02370;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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: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; AAHF01000015; EAL84657.1; -; Genomic_DNA.
DR RefSeq; XP_746695.1; XM_741602.1.
DR AlphaFoldDB; Q4WAS9; -.
DR SMR; Q4WAS9; -.
DR STRING; 746128.CADAFUBP00008646; -.
DR PRIDE; Q4WAS9; -.
DR EnsemblFungi; EAL84657; EAL84657; AFUA_7G02370.
DR GeneID; 3504252; -.
DR KEGG; afm:AFUA_7G02370; -.
DR VEuPathDB; FungiDB:Afu7g02370; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_2_1; -.
DR InParanoid; Q4WAS9; -.
DR OMA; ERCLYFE; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
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:0043486; P:histone exchange; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PS00690; DEAH_ATP_HELICASE; 1.
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..1695
FT /note="Helicase swr1"
FT /id="PRO_0000074363"
FT DOMAIN 334..408
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 842..1007
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1382..1532
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1590..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 958..961
FT /note="DEAH box"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..616
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1695
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 855..862
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1695 AA; 191097 MW; A83AF4D41401F81E CRC64;
MQDGSLNGLS HHNDERVNHE NEDKSLNTSA LGDSPDSANR ELIPSESKEN GVPTDSIEGP
PSKRRKLAGP DNSRRSTPRP PSPPWKKAGV DGPTSFLQDG KRRSSRVNAI PLELQPPSDK
RKTRAAQRST VNKNLSGNGK VVASSPLSMS VSQSGINGKH TGGNLTTGSP RTATPRGASA
RRRRISRSPP RQTPSRTRSQ SSATSAPNDP TSHNARSKRS HSNVTSTPTI GIDELWNDIG
GETDLGDEQG QRVPRLRIKV KKPVIGFQHP SHVIPPRKYN SFREWLESGE GRIEDGAVLT
PEAALVEARK RCRVLEATEP GGLLSPEVCS AYLPEQQEEP PQQYSHQDHL VAHALYFKKL
LDQEHRRHRN TARLLAQWCA DAWRKRNKRP EDILREQQEE VRVKRKQLAR DLQKMFDLAR
AEVDRMRLAR WEEERKVEDQ RALDRAIKQS TMLFEKRRLE ILGETGSDFL DSTDAEESGT
DATTSDAEED ESNMSSTDSE TEDEDEVDDD EGLTAEELRQ KYADLPQSSL VSDRESVASD
TSESSDGTRT SHILQNIEDI NDSQGETPLE QIELDEVDPM LLDDSEDEST DMDDDMGDSD
EDGDADGTDS DDESDDGPGL LGFFSSKDRV LNDAHRFDDE GDDPLAVSNH EGGSGFDDDG
QSVSVDEDGD EELEDADEVS LVPNGPSNSV SISQSTAEVS PVTETPDEEP DEQAEVVDTD
MAAAAPSEGP APLEASAPLE DLVAIDKRGD AMGECHRQQC SPLVNNLDEQ ELRQNGGASS
EASPGTLATK PSEPESISSF EAPGEKPPQP SESPAPGLKT PIPHLLRGTL REYQHYGLDW
LAGLYNNHIN GILADEMGLG KTIQTIALLA HLAVEHEVWG PHLVVVPTSV ILNWEMEFKK
WCPGFKIMTY YGSIEERRQK RKGWTDDTSW NVLITSYQLV LQDQQVLKRR NWHYMVLDEA
HNIKNFRSQK WQTLLTFRTR ARLLLTGTPL QNNLTELWSL LFFLMPSDGD GTGIEGFADL
RNFSEWFRRP VEQILEHGRE TMDDETKRVV TKLHTILRPY ILRRLKADVE KQMPAKYEHV
VYCRLSKRQR FLYDGFMSMA QTKETLASGN YLSIINCLMQ LRKVCNHPDL FETRQISTSF
VMHHSVATEY ASKEQLVRRR LLYEHPLTKL DLDFLNLVPI SREDISRRLA DDSTRLMAYG
PFNILRERQY KRTNWQMMFD GSTVQSTLEA LENDARKRRM AELERCLYFE SKRHGRRPVY
GTSLVEFLTA DSKQKPTLGG RPQTQSLAEW LSNRSSILAS MILSIEERSQ AMDGYVRRFA
CVTPAAVASG ITEAALTPIE TRYLTEKERF PPYDPFHEAQ MRLSIAFPDK RLLQYDCGKL
QRLDKLLRDL KAGGHRALIF TQMTKMLDIL EQFLNIHGHR YLRLDGTTKV EQRQILTDRF
NNDDRILVFI LSSRSGGLGI NLTGADTVIF YDLDWNPAMD KQCQDRCHRI GQTRDVHIYR
FVSEHTIESN ILRKANQKRM LDDVVIQEGE FTTDYFTKLD VRDMIGEEAE AQDEASAAMD
RVLSSRVATG GSRVFEQAED KEDIDAAKNA QKEMEQADND DFGDRSISHT PGQVGTPLAT
GPQEGETPGA QLITTPQIHG VDETVDVEPQ PGHIDDYLLR FMEWNMKDEP LVLPPDKTKK
KSKKGKEHRL SKRRR
