INO80_ASPOR
ID INO80_ASPOR Reviewed; 1444 AA.
AC Q2UTQ9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=AO090009000631;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007150; BAE55056.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UTQ9; -.
DR SMR; Q2UTQ9; -.
DR STRING; 510516.Q2UTQ9; -.
DR PRIDE; Q2UTQ9; -.
DR EnsemblFungi; BAE55056; BAE55056; AO090009000631.
DR HOGENOM; CLU_000315_26_0_1; -.
DR Proteomes; UP000006564; Chromosome 1.
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..1444
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350956"
FT DOMAIN 398..523
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 645..817
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1220..1380
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 207..283
FT /evidence="ECO:0000255"
FT COILED 440..511
FT /evidence="ECO:0000255"
FT MOTIF 768..771
FT /note="DEAQ box"
FT COMPBIAS 16..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 658..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1444 AA; 164774 MW; 3E104B45859DA52F CRC64;
MSFASILSGP AEERSPPKRQ SPPPETTPAP VTSTPREATQ LSPPPPPHVP PSHQKVKEQE
QVLPRLEKKP SSEKRRRNAE QDNKAGEPSN GILSNGIPEP TKTTTQSWSF LSPRKVLSER
ESETINKLMV EIDNAEKSDV EAPGFEEEYE QYKLQCKRRA LHTLKEEGIK RKRRRNTFLV
NLGKSLEKQA SAGMDRFRIA NEASVISEVQ AKEIQDEKER KKDMQRKRRR ENTVRLEMQK
KLEAERKANK AQDSAEKAKF LREAERAQRK IKTTKRALEG VTAPEEIGEV TPLAPNLEGG
TTSSFHIGRS SPSRRKSGRG GPVTRPKKSK EQKQAEKDAA EAAYAAMEND EPLPLAPKED
PRKESLKKEA KGSRSKESSP APLSAFETKG YNQIYEQIWR DIARKDIPKV YRIKALSLST
RQENLRKTAQ LASKQSRKWQ ERTNKSMKDT QARAKRTMRE MMSFWKRNER EERDLRRLAE
RQEIESAKKA EAEREANRQR RKLNFLISQT ELYSHFIGRK IKGAEGDSGD TAVEGSDETV
QPGKDEEHAM EDAGAKVTNF EDLDFDAEDE TALRQAAMAN AQNAVKEAQD RARAFNDGQD
HMAALDEGEL NFQNPTSLGD IEISQPTMLT AKLKEYQLKG LNWLVNLYEQ GINGILADEM
GLGKTIQSIS VMAYLAEVHN IWGPFLVIAP ASTLHNWQQE ITKFVPDIKV LPYWGSAKDR
KILRKFWDRK HITYTKESEF HVLVTSYQLV VLDAQYFQKV KWQYMILDEA QAIKSSQSSR
WKNLLGFSCR NRLLLTGTPI QNNMQELWAL LHFIMPTLFD SHDEFSEWFS KDIESHAQSN
TKLNEDQLKR LHMILKPFML RRVKKHVQQE LGDKVEKDVF CDLTYRQRAY YTNLRNRVSI
MDLIEKAAVG DEADSTTLMN LVMQFRKVCN HPDLFERAET KSPFSVAHFA ETASFVREGQ
NVDVGYSTRN LIEYPLPRLL CGSDGRVDVA GPGNLHAGFR GKYLAHLMNI FAPENIKHSA
EHDGTFSFLR FVDTSINEAY EQSHQGIFER AVRRRGKPNR LSRLNVVYDD DKATMASALP
HTMFNIVQRN DQHAINDVTT EGYMRELTTV AQSAFERKGL GIIEPCVSPA ASAPPITVSS
SSRAPLSEMN DSLFNVSVRH ALFSTPSKQL EQQILEKKLD PIPYSLPPML PQPISIKGRY
THIEVPSMRR FVTDSGKLAK LDELLRELKA GGHRVLLYFQ MTRMIDLMEE YLTYRNYKYC
RLDGSTKLED RRDTVADFQQ RPEIFVFLLS TRAGGLGINL TAADTVIFYD SDWNPTIDSQ
AMDRAHRLGQ TRQVTVYRLI TRGTIEERIR KRALQKEEVQ RVVISGGAAG GVDFNTRNRE
SRTKDIAMWL ADDEQAELIE QKEKEALDRG EVFGASKGGK KAAQKRKRDI TLDDMYHEVS
FAIH
