SWR1_EMENI
ID SWR1_EMENI Reviewed; 1698 AA.
AC Q5ARK3; C8VH70;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Helicase swr1;
DE EC=3.6.4.12;
GN Name=swr1; ORFNames=AN9077;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAA61910.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000169; EAA61910.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF82596.1; -; Genomic_DNA.
DR RefSeq; XP_682346.1; XM_677254.1.
DR AlphaFoldDB; Q5ARK3; -.
DR SMR; Q5ARK3; -.
DR STRING; 162425.CADANIAP00009538; -.
DR PRIDE; Q5ARK3; -.
DR EnsemblFungi; CBF82596; CBF82596; ANIA_09077.
DR EnsemblFungi; EAA61910; EAA61910; AN9077.2.
DR GeneID; 2868023; -.
DR KEGG; ani:AN9077.2; -.
DR VEuPathDB; FungiDB:AN9077; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_2_1; -.
DR InParanoid; Q5ARK3; -.
DR OMA; ERCLYFE; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..1698
FT /note="Helicase swr1"
FT /id="PRO_0000074368"
FT DOMAIN 329..403
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 837..1002
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1377..1527
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 953..956
FT /note="DEAH box"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..611
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 850..857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1698 AA; 190547 MW; FB023CCEF1AADA9D CRC64;
MQNGTTIGIP PENERVTERA EPVPSDLLPN NSPVNSPTID PTLSEIKDVA ADHNEEPPSK
RRKVAGSTPS RRSHSRAASP PWKKAGADGP TSKIVDGKRR STRVSNVGPV EQPPSDAKPT
RSSQKQYVSK AVSSQRNAAV SSPLPMSPSR SGINRRSLAG VAVNGSPSTT AKGSIGRRRR
ESPSPVSKRA STRTRPDNMD AYHPSNGVTP RSNSTKTRST RSFQLASSDF REETADDIGN
DGQDEHGQRI QRLRIKVKKP ALSIQHPSHV LPTRKYGSFK EWLENEGTGP GRMLTMTDAL
EEAQKRRQVT EAMEPGGLLS SEVCSAFLPE PQEELPQQFS HQDHLVAHAL YFKKLLDKEH
RAHRQAAKSL AAACAEVWRK RNKDPEDILR EQQEEMRGKR KQLAKDLKKM FELARAEIDR
VRLARWEEEQ KAKDQRALDR AIKQSTMLFE KRRLEILGET GSDAPETTTD DEEVETDNGS
ENDDEEGESN MSTETEEEDG DDRDDDVGLT AEELRLKYAN LPDTNPHPDQ SPYSDEDSED
SDDIAADNTP GDTSGGVNRS PPPDSSGQVE LDEVDPVLID DSDESTDMDD DMGDSDDDGY
SEAESDDEDG GEPGLLGFFS AKDLSLSNLH QTNSGEGDTH QTGADGDRNE DSSFDESEFG
SEDPDEVTLV PTGPTNKDLS TPATVTASAE LEPAAMTPSI DQTSTEEPIA IGTETPIETV
AEDAAALADT EPVDVDVLDT STNDSVPPVM SPATNLLKQI ERQQHEPYHS RAASSEASPG
TVATKPSEPE SVSSIEAPAE KHAQPSESPG PGLKTPIPHL LRGTLREYQH FGLDWLAGLY
SNHINGILAD EMGLGKTIQT IALLAHLAVE HGVWGPHLVV VPTSVILNWE MEFKKWCPGF
KIMTYYGNQE ERRQKRRGWM DDNSWNVLIT SYQLVLQDQQ VLKRRSWHYM ILDEAHNIKN
FRSQRWQALL TFRTRARLLL TGTPLQNNLT ELWSLLFFLM PTDGDEAGIE GFADLRNFSE
WFRRPVEQIL EHGRETMDDE AKQVVTKLHT VLRPYILRRL KADVEKQMPG KYEHVVYCRL
SKRQRYLYDG FMSRAQTKET LASGNYLSII NCLMQLRKVC NHPDLFETRP ISTSFAMPRS
VATEFETSEA LVRRRLLYQH PLEKLDLDFL NLVPISREDI SRRLADDSAR IMAYAPFNTL
RERQYHRTNW EMKFNGSTVQ STLEALENDC RKRRMAELER SLYFESKRHG RRPVYGSSLI
EFLTADSKQR PTAHGPLRKR SYADWLSSQS SVLASMMMSL EERSQAMDGY IQRFACVTPA
AVAAGVTEAA LTPISTRHLT NKERFPPHDP FHEAQMRLSI AFPDKRLLQY DCGKLQRLDK
LLRDLKAGGH RALIFTQMTK MLDVLEQFLN IHGHRYLRLD GTTKVEQRQI LTDRFNNDNR
ILAFILSSRS GGLGINLTGA DTVIFYDLDW NPAMDKQCQD RCHRIGQTRD VHIYRFVSEY
TIESNILRKA NQKRMLDDVV IQEGEFTTDY FTKLDVRDMI GNDEALKDEA SAAMDRVLEN
RVTNTSRVFE QAEDKEDIDA AKNAQKELEH ADDGDFDDRA NANASGVTAA SASASGAGQT
PTQAGTPLPD EAQQSLNANN AEVAEDTADS DPSVGHIDDY LLRFMEWNMK DEPLVLPVDK
SMKKSKKGKE HRLRKRRR
