INO80_EMENI
ID INO80_EMENI Reviewed; 1612 AA.
AC Q5BAZ5; C8VN32;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=AN2285;
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: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair.
CC {ECO:0000255|PROSITE-ProRule:PRU00746}.
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;
CC Evidence={ECO:0000250|UniProtKB:P53115};
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AACD01000038; EAA64396.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86533.1; -; Genomic_DNA.
DR RefSeq; XP_659889.1; XM_654797.1.
DR AlphaFoldDB; Q5BAZ5; -.
DR SMR; Q5BAZ5; -.
DR STRING; 162425.CADANIAP00008977; -.
DR EnsemblFungi; CBF86533; CBF86533; ANIA_02285.
DR EnsemblFungi; EAA64396; EAA64396; AN2285.2.
DR GeneID; 2874790; -.
DR KEGG; ani:AN2285.2; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR InParanoid; Q5BAZ5; -.
DR OMA; DDMYHEG; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:EnsemblFungi.
DR GO; GO:0032006; P:regulation of TOR signaling; IEA:EnsemblFungi.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR031047; Ino80.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; PTHR45685:SF2; 1.
DR Pfam; PF13892; DBINO; 1.
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; PS51413; DBINO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1612
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074324"
FT DOMAIN 570..695
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 810..982
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1325..1485
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..455
FT /evidence="ECO:0000255"
FT COILED 612..684
FT /evidence="ECO:0000255"
FT MOTIF 933..936
FT /note="DEAQ box"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 823..830
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1612 AA; 181601 MW; 236745D04E357BB5 CRC64;
MTGAPPYHPQ SPTQQSHYAG YSPSNKPRHY YPNSEHYQQQ PPQTPPAFPQ PNLARSPHYS
HAPSPLPGAL PPLNGGAPTP AHPSDPSPQY QAHSAAGTPQ YPLPRPYSGS LLPASGTSPY
GPSTPSHAHP SSRPDSHAHV SPKKEPESHF AVNHGAPAYS VMREPQASPP KEAKPARAAD
PMSFASILSG PTEEQAPPKI QSPTPGLGTI HSAVPAANAT SLNPPPASFH PKVGDIEPVP
PVSAPRLEKK PSADKRQRNT EKEDLKSAEN PTNGVTEPPK ILRPPRRIMS EKETEMVNKY
MVEIDNAEKS DVEAPGFEQE RERYILKGKK RALDVERAES IRRKRRRHDY LLKLGKSFEK
QANAGMDRFR YANEASVISE VQAKEIQDEK ERKKDMQRKR RRENTVRMEM QKKLEAELKA
NETQDSAEKA KFLREAERAQ RKIKTTKRAL EGVTEPEEIG EITPLAPNLE GGITSSFHIG
RSSPSRRKTG RGGPVTRPKK SKEQKQAEKD AAEAAYAAME NDEPLPLAPR EDPRKESLKK
DAKGGRSKEA TPVPVSTYES KGYNQIYEQI WRDIARKDIP KVYRTKVNSL STRQENLRKT
AQLASKQSRK WQERTNKSMK DTQARAKRTM REMMSFWKRN EREERDLRRL AEKQELESAK
RAEAEREANR QKRKLNFLIS QTELYSHFIG RKIPGAGGES GDAGVQGTEA MDLTPGAGAK
VTNFEDLDFD AEDDTALRQA AMANAQSAVQ KAQERARAFD DPNKSTMDTM DDSELNFQNP
TSLGDIEISQ PTMLTAKLKE YQLKGLNWLV NLYEQGINGI LADEMGLGKT IQSISVMAYL
AEVHNIWGPF LVIAPASTLH NWQQEITKFV PNIKVLPYWG NAKDRKILRK FWDRKHITYT
KESEFHVLVT SYQLVVLDAQ YFQKVKWQYM ILDEAQAIKS SQSSRWKSLL GFHCRNRLLL
TGTPIQNNMQ ELWALLHFIM PTLFDSHDEF SEWFSKDIES HAQSNTKLNE DQLRRLHMIL
KPFMLRRVKK HVQQELGDKV EKDVFCDLTY RQRALYTNLR NRVSIMDLIE KAAVGDETDS
TTLMNLVMQF RKVCNHPDLF ERAETKSPFS LAHFAETASF NIKQSIEDDG AFSFLRFVDT
SVGEAFNYSH QGVFERALRR RGQTNRLSRL SVVYDEDESS TATLPHTLFN IVDRNDRQAV
YDIAVEGHMR ELMNVSRSVF EQEGLNVIEP CAGPAASAPP ITLVSSGQEA LIETQDALFN
VPVQHALFGT PSKAMEEQII EQQLDPTPYS LPPMLPEPIS TKGRYTHIEV PSMRRFVTDS
GKLAKLDELL RELKAGGHRV LLYFQMTRMI DLMEEYLTYR NYKYCRLDGS TKLEDRRDTV
ADFQQRPDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP TIDSQAMDRA HRLGQTRQVT
VYRLITRSTI EERIRKRALQ KEEVQRVVIS GGAAGGVDFN TRNRDSKTKD IAMWLADDEQ
AELIEQKERE ALERGETFGA SKGGKKNAQK RKRDVTLDDM YHEGEGNFDD ASAKPSGAAT
PVSTAENIGT PSASTPVPKR GRGRGGKGTA KRAKTTKERL RLIDGDGGLG SG
