SWR1_GIBZE
ID SWR1_GIBZE Reviewed; 1691 AA.
AC Q4IAK7; A0A0E0SKV3; V6RAW2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Helicase SWR1;
DE EC=3.6.4.12;
GN Name=SWR1; ORFNames=FGRRES_05751, FGSG_05751;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; DS231665; ESU11758.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF87066.1; -; Genomic_DNA.
DR RefSeq; XP_011324334.1; XM_011326032.1.
DR AlphaFoldDB; Q4IAK7; -.
DR SMR; Q4IAK7; -.
DR STRING; 5518.FGSG_05751P0; -.
DR PRIDE; Q4IAK7; -.
DR EnsemblFungi; ESU11758; ESU11758; FGSG_05751.
DR GeneID; 23552917; -.
DR KEGG; fgr:FGSG_05751; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G18675; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_2_1; -.
DR InParanoid; Q4IAK7; -.
DR Proteomes; UP000070720; Chromosome 3.
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; 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; 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..1691
FT /note="Helicase SWR1"
FT /id="PRO_0000074369"
FT DOMAIN 335..409
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 823..988
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1375..1525
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 939..942
FT /note="DEAH box"
FT COMPBIAS 50..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..612
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1691
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 836..843
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1691 AA; 190422 MW; CB6C314827589965 CRC64;
MPETASTANV LPKSDPDAIK TEQDALEGYE NGGDALQGTM DGHVETNGDA PATENHHEPN
HIHDDERPAK RRRTRDSTPP QNTPKKMKPV SPPWKKISAD GPTSYTENGR RKSGRINTLL
PEPSPLSKSR TSKRSTGANS NTKTEIHLTN GNSRKMPNGS HKASPATKAP SKQAPASTPK
SASKKPTETR TSSRSTRRRS PTPPPPPKNS TRSRRSARFS DAVIKDEAVQ DSRTATSNST
NRSPRIKLRV GRSGHIPLVH PGQVRKRPKI GTSFEDFWTR AGDIPVEEGG LQASEDGPQY
TDELAERDAR VILRVEKEVE DGGMLSQGRC SIFLPEPAEE PPRQWARQDH MVKAMTNFRK
LMLAEQQRHR IAAKKVAEAC RDEWLRRQPK SEEEIEAEQR AVWISRYRIV AKTLFGTWEN
VRTEVNRRRL AEWEQEEQRR VKAALNEAVN LSEQKLQARQ AGLDSEQLSE EDGFDDLSDD
MSMADDDELG LASGEDEDDE DGDADSDIMS SDEEEGDEED QKDIGDENLT QEQLRAKYAH
IPELEKPSTE TPVTEPTPKD TDAVDTAQAT ATENAETSDE SVDMDDDMGS TDMDSDEEDE
EEESEEESDE DAGGLLGLLF GKSELKKMNS EAVAETPADS KEDSEMPDVE AVSDGEGAEE
NEMSLIQMPD PEPHESGALE KSTKEAVEEK EQIPAAMQDV AAGQDGLSNT DNNVQEPASQ
DNDVAMTGND PEEPSALTFE KPHSPATEPA TNPPSRVHST SPPATSETKP SELDTASTEE
MAVDKHDTSR SPSPQPSNHK IEVPFLLRGT LREYQRDGLD WLAGLYANST NGILADEMGL
GKTIQTIALL AHLACTHEVW GPHLVIVPTS VMLNWEMEFK KWCPGFKILA YYGSQEERKR
KRQGWNNDDI WNVCITSYQL VLQDQQVFKR RRWHYMILDE AHNIKNFKSQ RWQTLLGFNT
QARLLLTGTP LQNNLTELWS LLFFLMPAEN GVGGFADLQE FHDWFAKPES QILESGREQM
DDEARAIISK LHKVLRPYLL RRLKADVEKQ MPAKYEHVEF CRLSKRQREL YDGFLSRTDT
KETLNSGNYL SIINCLMQLR KVCNHPDLFV DRPIMTSFRM QKSVVSDFEV TEQRVQRLLH
DPSPMKDVSL GFLNLMPTQC ESLSTTQAER ISQLSSHRKL MELREAQKIR AQSAHANLDP
STVASNIGYL ESGARWGRYE ELQHCVYLNA LRRQKKPIYG KNLIELLTIG TDKRPYKPRP
KIPRQVLAWF EEESTLVQSM IPTVNQRADS FKTIIEKFSC VTPAVVTRDM EQFVLGRKGI
EAFSDEDLKL SAPVRWAPFL PKEAPPDPWH EGRMRLSIQF PDKRLLQYDC GKLQILDKLL
RKLQAGGHRA LIFTQMTKVL DILEQFLNIH GHKYLRLDGA TKVEQRQILT DRFNNDPRIL
CFILSTRSGG LGINLTGADT VIFYDQDWNP AMDKQCQDRC HRIGQTRDVH IYRLVSEHTI
EANILRKASQ KQMLDDVVIQ EGEFTTDYFN KLSVRDVLSE KLDSKSEGLD AADAALDRVL
GGPDTNNDQR RVGRALEQAE DREDVAAARV AEKEIQADDA DFTEKPSNNA SGTSTARQGT
PAGKSVLDGG LDDIDAPHVE EVLEYNAWGD KMHTIDDYML GIMAEQLKDT KLELPKDKKK
GKKKGKDTRK R
