ID   INO80_CANGA             Reviewed;        1484 AA.
AC   Q6FV37;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=INO80; OrderedLocusNames=CAGL0E05038g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380951; CAG58826.1; -; Genomic_DNA.
DR   RefSeq; XP_445907.1; XM_445907.1.
DR   AlphaFoldDB; Q6FV37; -.
DR   SMR; Q6FV37; -.
DR   STRING; 5478.XP_445907.1; -.
DR   PRIDE; Q6FV37; -.
DR   EnsemblFungi; CAG58826; CAG58826; CAGL0E05038g.
DR   GeneID; 2887378; -.
DR   KEGG; cgr:CAGL0E05038g; -.
DR   CGD; CAL0128574; CAGL0E05038g.
DR   VEuPathDB; FungiDB:CAGL0E05038g; -.
DR   eggNOG; KOG0388; Eukaryota.
DR   HOGENOM; CLU_000315_26_2_1; -.
DR   InParanoid; Q6FV37; -.
DR   OMA; FWKKNER; -.
DR   Proteomes; UP000002428; Chromosome E.
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..1484
FT                   /note="Chromatin-remodeling ATPase INO80"
FT                   /id="PRO_0000074321"
FT   DOMAIN          493..618
FT                   /note="DBINO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT   DOMAIN          734..906
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1299..1463
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          149..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          404..462
FT                   /evidence="ECO:0000255"
FT   MOTIF           857..860
FT                   /note="DEAQ box"
FT   COMPBIAS        154..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..336
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1468..1484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         747..754
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1484 AA;  170540 MW;  A6CB2876E014F1F2 CRC64;
     MSLSALLNND DPVEDTKLYL ESLNREMDRL IKRDQLELMY QDWKFANYQE FELISEWNTQ
     CKELVGDGND LQNNDLMTEE VHLDDLYDNI QRIRNEWKDY ESYKETRSQL LSKSIQAKPI
     KHRRRRRTKL EMEAAANLAA LSQMGTTDVK TPEIINDHGN RSKASRSDTT NKTDNTMAGI
     NSPTSDVDSG HKDELDQTKL IKKQEASSST NSAASVTASV ANGIVEDQKD EAERTIEANR
     IGSNMQNSDQ DTMDDLKKTN DPSSDIDSDA NTSVNDGSDE NLSNKLDSDD LHSEPADNEE
     EPVSSDAEKD QAENINQTDE SEEEIIVKEY DDNNDEDFAP EIKKPKPNGK IVTINSDRPK
     IVRELIKLRN KGKAPKSSKR RYTAVNITEY SPTEKKISVK ITLKQMHVKK LKKILQDARK
     AEEKRLQEEA KQIADQESPR KRRKIDRSEN TKQEDEDDKE DDDLDGLPTY GMKMSLKDAK
     AIQRHYDNTY TMIWKDMARK DCMKISRLVQ QIQSTRALNY KKTSSLCARE ARKWQTRNFK
     QVKDFQTRAR KGIREMANFW KKNEREERDL KKKAEREALE LAKKEEEEKE SKRQAKKLNF
     LLTQTELYSH FIGRKIKTSA LEGNEVAEED EDNYDLTTTA PNKNDFHAID FDNENDEQLK
     LKAAQNASNA LAETRAKAKA FDDAHRQQQS TESDDEEEMN FQNPTSLGEI TIEQPKMLAC
     TLKEYQLKGL NWLANLYDQG INGILADEMG LGKTVQSISV LAHLAEHHNI WGPFLVVTPA
     STLHNWVNEI SKFVPQFKIL PYWGSANDRK VLRKFWDRKN LRYSEKSPFH VMITSYQMVV
     ADASYLQKMK WQYMILDEAQ AIKSSQSSRW KNLLSFHCRN RLLLTGTPIQ NNMQELWALL
     HFIMPSLFDS HDEFNEWFSR DIESHAEGNS SLNQQQLRRL HMILKPFMLR RIKKNVQSEL
     GDKIEIDVMC DLTQRQTKLY QVLKSQMSSN YDAIENAAAE GSDIAGGGNS DQSIINAVMQ
     FRKVCNHPDL FERADINSPF SFTSFGKTSS LISSSIATSG GLTETISELM YSSTNPINCA
     IPKLIYEDLI LPNYNNSIDI MEKLLLSDFS IYDPVNNKEM CQYLGLLTGL AYGSFRKIHK
     SNYFERIINL KKESKQSSQN LITVVSNAND LIADSIVHAD TNLPNLTGIR NDIYHNDYLN
     SIQPGYCPKV VAPPINFNVN GSLNFTNKMS SYLFNPVITT ALSSIPPPTQ YNMFVKKCIP
     IEEFPISEMY PNPLNKHFSS NISMPSMDRF ITESAKLKKL DELLVELKKN DHRVLIYFQM
     TKMMDLMEEY LTYRQYNHIR LDGSSKLEDR RDLVHDWQTN PEIFIFLLST RAGGLGINLT
     AADTVIFYDS DWNPTIDSQA MDRAHRLGQT KQVTVYRLLV RGTIEERMRD RAKQKEQVQQ
     VVMEGKTKDT NIQTTHTRPE HEQLTPKSLS SEPEATNNLI TVKN