INO80_ASPNC
ID INO80_ASPNC Reviewed; 1697 AA.
AC A2R9H9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=An17g01490;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270389; CAK43045.1; -; Genomic_DNA.
DR RefSeq; XP_001398378.1; XM_001398341.1.
DR AlphaFoldDB; A2R9H9; -.
DR SMR; A2R9H9; -.
DR PaxDb; A2R9H9; -.
DR EnsemblFungi; CAK43045; CAK43045; An17g01490.
DR GeneID; 4989472; -.
DR KEGG; ang:ANI_1_210154; -.
DR VEuPathDB; FungiDB:An17g01490; -.
DR HOGENOM; CLU_000315_26_1_1; -.
DR Proteomes; UP000006706; Chromosome 5L.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IEA:EnsemblFungi.
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..1697
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350955"
FT DOMAIN 581..706
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 835..1007
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1410..1570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..466
FT /evidence="ECO:0000255"
FT COILED 623..694
FT /evidence="ECO:0000255"
FT MOTIF 958..961
FT /note="DEAQ box"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 848..855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1697 AA; 190332 MW; 209298229D2CCEB1 CRC64;
MTGAPPYNPQ SPTQQSRYPV YSPPAKSRPY YANNEQYQQH PPQTPPAFSS RSPHFSHAPS
PLPGTLPPLN GAAPPSSHPS EPPSQYQAHS SAGNPQFALP RPYPGSVLSG NGASPYGHST
PSHAHPAGRP DSHPQTSPKK ESESQFPMST HGVMGYPSSV VREPRASSPP KDVKPTRAAD
PMSFASILSG PTEERAPPPR QSSAEATPTP LAPAATAQTS LSPPPVASAA TSQKSKDRAP
ALTASLPRLE KKPTTEKRRR NPPETEQKTA DSRTSNVANG VSEPSKTLAQ PRGAGSRPVM
SERETEALNK ALADMAEADK SDVEAPGYDR FREEYRAKGK KRAFATEQAE ILRRKRRRND
FLVKLSKSLE KQATAGMDRF RYANEASVVA EVQAKEIQDE KERKKDMQRK RRRENTVRME
MQKKKEAEAK AHEAQDSAEK AKFLREAERA QRKIKTTKRA LEGITAPEEI SEVTPLAPNL
EGGTTSSFHI GRGSPSRRKS GRGGPVTRPK KSKEQKQAEK DAAEAAYAAM ENDEPLPIAP
KEDPRKESLK KEVKGGRSKE PTPTPLSAYE TKGYNQIYEQ IWRDIARKDI PKVYRIKALS
LSTRQENLRK TAQLASKQSR KWQERTNKSM KDTQARAKRT MREMMSFWKR NEREERDLRR
LAEKQEIESA KKAEAEREAN RQRRKLNFLI SQTELYSHFI GRKIKGAEGD AAGDTAVEAT
GETVQPGKGQ DHTIDMPSSV ADAGTKVTNF EDLDFDAEDE TALRQAAMAN AQNAVQEAQD
RARAFNSGQN QMDALDEGEL NFQNPTSLGD IEISQPNMLT AKLKEYQLKG LNWLVNLYEQ
GINGILADEM GLGKTIQSIS VMAYLAEVHN IWGPFLVIAP ASTLHNWQQE ITKFVPDIKV
LPYWGSAKDR KILRKFWDRK HITYTKESEF HVLVTSYQLV VLDAQYFQKV KWQYMILDEA
QAIKSSQSSR WKNLLGFHCR NRLLLTGTPI QNNMQELWAL LHFIMPTLFD SHDEFSEWFS
KDIESHAQSN TKLNEDQLRR LHMILKPFML RRVKKHVQQE LGDKVEKDIF CDLTYRQRAY
YTNLRNRVSI MDLIEKAAVG DEADSTTLMN LVMQFRKVCN HPDLFERAET KSPFSTAYFA
ETASFVREGN NVDVRYSTRN LIEYPMPRLL CGAGGRVDVA GAENPHAGFR GRYLNHLMNI
FTPENMKQSI QDDGAFSFLR FVDTSLGEAY EQSHLGIFER AVRRRGQVNR LSRLNVAYDD
DKELAGSALP HTLFNIVDRN DKHAVNEVAA EGIMRDLMTV SQSTYEREGL NIIEPCVSPA
ASAPPISVVS SSHIPSIETR DTLFNVSVRH ALYSTPSRQV DEQIIEKKVD PTPYSLAPML
PKPISAKGRY THIEVPSMRR FVTDSGKLAK LDELLRELKA GGHRVLLYFQ MTRMIDLMEE
YLTYRNYKYC RLDGSTKLED RRDTVADFQQ RPEIFVFLLS TRAGGLGINL TAADTVIFYD
SDWNPTIDSQ AMDRAHRLGQ TRQVTVYRLI TRGTIEERIR KRALQKEEVQ RVVITGGAAG
GVDFNTRNRE SRTKDIAMWL ADDEQAELIE QKEKEALDRG EVFGAGKGGK KAAQKRKKDI
TLDDMYHEGE GNFDDASAKP SGAATPVSTA ENVGTPSSTP APKRGRGRGS GKGTSKRAKT
TKERLRLIDG DGGLGPS
