INO80_ASPTN
ID INO80_ASPTN Reviewed; 1690 AA.
AC Q0CA78;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=ATEG_09406;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476607; EAU30543.1; -; Genomic_DNA.
DR RefSeq; XP_001218028.1; XM_001218027.1.
DR AlphaFoldDB; Q0CA78; -.
DR SMR; Q0CA78; -.
DR STRING; 341663.Q0CA78; -.
DR EnsemblFungi; EAU30543; EAU30543; ATEG_09406.
DR GeneID; 4353733; -.
DR VEuPathDB; FungiDB:ATEG_09406; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR OMA; DDMYHEG; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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..1690
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350957"
FT DOMAIN 581..706
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 830..1002
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1403..1563
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..468
FT /evidence="ECO:0000255"
FT COILED 623..694
FT /evidence="ECO:0000255"
FT MOTIF 953..956
FT /note="DEAQ box"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
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 1635..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 843..850
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1690 AA; 189823 MW; F9D1FA717A4BF0A5 CRC64;
MSGAPPYNPQ SPTQQSRYPV YSPPNKNRPF YSNNDQYQQH PPHTPPAYPS QPAAMSRSPH
HPHAQSPLPG TLPPLNGAAP PPHHPDASSQ FQPHAAAGTP QYSLPRPYSG SVLSSNGTTP
YGPSTASHAH PSARPDGPPH LSPKKEMEPS FSMGSHGVPG YPPSAMREPR LASPPKEVKP
ARAADPMSFA SILSGPTEDR PPPRKPSPPE VAPAPLALAP ASAARQSPPL PISARAPPLS
KEPEPAPVTP LPRLEKKPSS EKRRRNVDQE PKMGELSVPP TNGLLDPAKA AVQPRAPPRK
TLSERETEYI NRVMAELDSM EKSDVESPGF EWELERYTAK GKKRAMDAER AESVRRKRRR
HDFLIKLGKT FEKQASAGMD RFRMANESSV VAEVQAKEVQ DEKERKKDMQ RKRRRENTVR
LEMQKKLEAE RKANKAQDSA EKAKFLREAE RAQRKIKTTK RALEGVTAPE EIGEVTPLAP
NLEGGTTSSF HIGRSPSRRK SGRGGPVTRP KKSKEQKQAE KDAAEAAYAA LENEELLPLA
PRDDRKDVLR KDGKGVLSKE ATPIPLSSYE SKGYNQIYEQ IWRDIARKDI PKVYRIKVLS
LSTRQENLRK TAQLASKQSR KWQERTNKSM KDTQARAKRT MREMMSFWKR NEREERDLRR
LAEKQEIESA KKAEAEREAN RQRRKLNFLI SQTELYSHFI GRKIKGAEGD ESGDTAVEGA
NEAAQSKMDV PAGALKAGAG VTNFEDLDFD AEDETALQQA AMANAQNAVQ QAQDRARAFN
NTKDDPMAAM DEGELNFQNP TSLGDIEISQ PSMLTAKLKE YQLKGLNWLV NLYEQGINGI
LADEMGLGKT IQSISVMAYL AEVHNIWGPF LVIAPASTLH NWQQEITKFV PDIKVLPYWG
SAKDRKILRK FWDRKHITYT KESEFHVLVT SYQLVVLDAQ YFQKVKWQYM ILDEAQAIKS
SQSSRWKNLL GFHCRNRLLL TGTPIQNNMQ ELWALLHFIM PTLFDSHDEF SEWFSKDIES
HAQSNTKLNE DQLKRLHMIL KPFMLRRVKK HVQQELGDKV EKDVFCDLTY RQRAYYTGLR
DRVSIMDLIE KAAVGDEADS TTLMNLVMQF RKVCNHPDLF ERAETKSPLT TAYFAETASF
VREGQFVDVG YSTRSLIEYP LPRLLCSSAG RVDVAGPDNL HAGFRGKYLA HMMNVFAPEN
IKQSIQEDGA FSFLRFIDTS MGDAYEQSHR GVFERALSRR GQPNRLSRLN VVYEEDEGDA
PLAHTMLNIV ARNDQSAVHE ITPDGYMREL MTVSQSTFER EGLNVIEPCA SPAASAPPVT
ITSSSPAAQI EMSDALFNVP VRHALFSTPT RQLEEQILEK KLDPVPYSHP PMLPKPTSLK
GRYTHIEVPS MRRFVTDSGK LAKLDELLRE LKAGGHRVLL YFQMTRMIDL MEEYLTYRNY
KYCRLDGSTK LEDRRDTVAD FQQRPEIFVF LLSTRAGGLG INLTAADTVI FYDSDWNPTI
DSQAMDRAHR LGQTRQVTVY RLITRGTIEE RIRKRALQKE EVQRVVITGG AAGGVDFNTR
NRESRTKDIA MWLADDEQAE LIEQKEKEAL DRGEVFGASK GGKKAAQKRK RDITLDDMYH
EGEGNFDDAS AKPSGAATPV STADVGGTPS STPVPKRGRG RGTGKGTSKR AKTTKERLRL
IDGDGGLGPM
