INO80_YEAS7
ID INO80_YEAS7 Reviewed; 1495 AA.
AC A6ZU34;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
DE AltName: Full=Inositol-requiring protein 80;
GN Name=INO80; ORFNames=SCY_1917;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair. Its
CC ability to induce transcription of some phosphate-responsive genes is
CC modulated by inositol polyphosphates. The INO80 complex is involved in
CC DNA repair by associating with 'Ser-129' phosphorylated H2A histones as
CC a response to DNA damage. {ECO:0000250|UniProtKB:P53115}.
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 chromatin-remodeling INO80 complex, at least
CC composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3,
CC IES4, IES6, ACT1, IES2, IES5 and INO80. {ECO:0000250|UniProtKB:P53115}.
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; AAFW02000099; EDN61972.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZU34; -.
DR SMR; A6ZU34; -.
DR PRIDE; A6ZU34; -.
DR EnsemblFungi; EDN61972; EDN61972; SCY_1917.
DR HOGENOM; CLU_000315_26_2_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Transcription;
KW Transcription regulation.
FT CHAIN 1..1495
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350966"
FT DOMAIN 482..607
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 724..896
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1309..1473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 137..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 847..850
FT /note="DEAQ box"
FT COMPBIAS 138..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 737..744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53115"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53115"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53115"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53115"
SQ SEQUENCE 1495 AA; 172093 MW; 0EB8F56CE2DF5DAA CRC64;
MSLAVLLNKE DKDISDFSKT TAGKSAKKNS RERVADVAPT RVLDKKQAYL SQLNSEFNRI
KKRDSIEQLY QDWKFINLQE FELISEWNQQ SKDWQFDNTN DSQDLHFKKL YRDMSMINKE
WAEYQSFKNA NLSDIINEKD ADEDEEDDED ELEDGEEDME EDEASTGRHT NGKSMRGNGI
QKSRKKDAAA AAAVGKAIKD DQTHADTVVT VNGDENEDGN NDEDNDNDNE NNNDNDNDND
NDNDNDNENE NDNDNDNDDE EENGEEDEEE EEIEDLDEED FAAFEEQDDN DDEDFNPDVE
KRRKRSSSSS SSTKLSMNSL SLITSKKINK NITINSDRPK IVRELIKMCN KNKHQKIKKR
RFTNCIVTDY NPIDSKLNIK ITLKQYHVKR LKKLINDAKR EREREEALKN NVGLDGNDLD
NDEDGSESHK RRKLNNNTAN GADDANKRKF NTRHGLPTYG MKMNAKEARA IQRHYDNTYT
TIWKDMARKD STKMSRLVQQ IQSIRSTNFR KTSSLCAREA KKWQSKNFKQ IKDFQTRARR
GIREMSNFWK KNEREERDLK KKIEKEAMEQ AKKEEEEKES KRQAKKLNFL LTQTELYSHF
IGRKIKTNEL EGNNVSNNDS ESQKNIDISA LAPNKNDFHA IDFDNENDEQ LRLRAAENAS
NALAETRAKA KQFDDHANAH GEEEEEDELN FQNPTSLGEI TIEQPKILAC TLKEYQLKGL
NWLANLYDQG INGILADEMG LGKTVQSISV LAHLAENHNI WGPFLVVTPA STLHNWVNEI
SKFLPQFKIL PYWGNANDRK VLRKFWDRKN LRYSKNAPFH VMVTSYQMVV TDANYLQKMK
WQYMILDEAQ AIKSSQSSRW KNLLSFHCRN RLLLTGTPIQ NSMQELWALL HFIMPSLFDS
HDEFNEWFSK DIESHAEANT KLNQQQLRRL HMILKPFMLR RVKKNVQSEL GDKIEIDVLC
DLTQRQAKLY QVLKSQISTN YDAIENAATN DSTSNSASNS GSDQNLINAV MQFRKVCNHP
DLFERADVDS PFSFTTFGKT TSMLTASVAN NNSSVISNSN MNLSSMSSNN ISNGKFTDLI
YSSRNPIKYS LPRLIYEDLI LPNYNNDVDI ANKLKNVKFN IFNPSINYEL CLFLSKLTGE
PSLNEFFRVS NTPLLKRVIE RTNGPKNTDS LSFKTITQEL LEVTRNAPSE GVMASLLNVK
KHAYEREYLN CIQRGYHPNV SAPPVTIEVL GSSHVTNSIN NELFDPLISQ ALSDIPAITQ
YNMHVKKGIP VEDFPKTGLF PEPLNKNFSS NISTPSMDRF ITESAKLRKL DELLVKLKSE
GHRVLIYFQM TKMMDLMEEY LTYRQYNHIR LDGSSKLEDR RDLVHDWQTN PEIFVFLLST
RAGGLGINLT AADTVIFYDS DWNPTIDSQA MDRAHRLGQT RQVTVYRLLV RGTIEERMRD
RAKQKEQVQQ VVMEGKTQEK NIKTIEVGEN DSEVTREGSK SISQDGIKEA ASALA
