ID   INO80_MAGO7             Reviewed;        1944 AA.
AC   A4R227; G4MLP8;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=INO80; ORFNames=MGG_06776;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001231; EHA56881.1; -; Genomic_DNA.
DR   RefSeq; XP_003709493.1; XM_003709445.1.
DR   AlphaFoldDB; A4R227; -.
DR   SMR; A4R227; -.
DR   STRING; 318829.MGG_06776T0; -.
DR   PRIDE; A4R227; -.
DR   EnsemblFungi; MGG_06776T0; MGG_06776T0; MGG_06776.
DR   GeneID; 2684949; -.
DR   KEGG; mgr:MGG_06776; -.
DR   VEuPathDB; FungiDB:MGG_06776; -.
DR   eggNOG; KOG0388; Eukaryota.
DR   HOGENOM; CLU_000315_26_1_1; -.
DR   InParanoid; A4R227; -.
DR   OMA; DDMYHEG; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
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:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
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; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW   Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1944
FT                   /note="Chromatin-remodeling ATPase INO80"
FT                   /id="PRO_0000350960"
FT   DOMAIN          840..965
FT                   /note="DBINO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT   DOMAIN          1090..1262
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1663..1818
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1862..1944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          506..563
FT                   /evidence="ECO:0000255"
FT   COILED          624..696
FT                   /evidence="ECO:0000255"
FT   COILED          908..953
FT                   /evidence="ECO:0000255"
FT   MOTIF           1213..1216
FT                   /note="DEAQ box"
FT   COMPBIAS        16..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..427
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..983
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1103..1110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1944 AA;  218298 MW;  EA1E1E1DE1916A0D CRC64;
     MEPSKFHSTV LARPPGMYDE DDDHRRRQRD ILNPPAPSQT GPGSGGSSSA GGPRPPFSLR
     SPTQSEFHHQ SSQHHYSASS AASGPQSTYN GANNGVPQSH SHSRSNSHSR HSSSSVLHSP
     YQQASTASRP AHALDLHRSP QTSGLQAPQR SPGLHAPSVY YSQESREHHP PPPKPIDKPA
     SSGRSFYDPL TDTTTTSTSD RERRTSDAGS SWHNATTNAV STPTHRDAYN SYSKPAANPS
     PYYGNGKYTS PSASIYPPRS PASHPQSVAT AAAEPISPPT RPPRMATPNI LNPTTTSSMA
     AMSQAESPAQ KAAVPAATPS RAAELMSFSN ILSSSEPAPK PRPRSPVLAE TPNKQPEPEP
     EREPTKEPSK EPSKEPSKEP SKEPSPPPAD MDETSDSPAC PEKPAEVDAE TEPDAEIHDD
     VDTVDGLEES EKPEPPIKRE KSAKVEKAPR RPRVVEKEKK ERVTKAPRKS AGAKGRASEV
     KAESTPKQSR RSSGKQEALS SSRVPAKRQA NGLTKQKAQA LEQEKAVVAE MEQLEEEALD
     ESEARAELRA FKKRKLNRQK ALETTDLSVA TELLPSLKDE AINRHHRRHD FSAEMVLKLG
     VHVALGRLRF GDHNYDAALK EVREQELFAE KERKKDMQRK RRREKSMAVT IEQKEAALAK
     AHATEDKLER QKLLREAERA NKKAQQTKLI LQKGIKGPAR NIMPMDVNLE GGSMATFSAD
     SMEPGKGKGK GRAGNRPKKS KEQKQAEKEA AEAAQAALDA GQELPSKEEN PKIRIKVNKG
     KLSKDKDRDV DVDTIDGDNT EIKDTEEPPP KKKGKVVEEV KDTLETRFQS KGYNQIYDQI
     WRDMARKDVS KVYRLATDSY YTKASNLKKT AILAAKEAKR WQLRTNKGMK DLQARGKRVM
     RDMMTFWKRN EREERDLRKA AERQELENAR KEEADREAAR QKRKLNFLIS QTELYSHFIG
     KKIKTDEVER STDRPEVAAE EQKNKPAGEN ALTVKEPTGP VGAKVTNFEN LDFDAEDDET
     LQAAAMANAQ NAIAEAQRKA RNFNNDDEPD EDGEMNFQNP TGLGDVEIEQ PKLLTATLKE
     YQLKGLNWLV NLYEQGINGI LADEMGLGKT IQSISVMAYL AEHHDIWGPF LVVAPASTLH
     NWEQEIKRFV PDLKIVPYWG SASDRKILRK FWDRKHSTYK RDAQFHVAIT SYQMVVSDVA
     YFQKMKWQYM ILDEAQAIKS SQSSRWKCLL SFHCRNRLLL TGTPIQNNMQ ELWALLHFIM
     PSLFDSHEEF SDWFSKDIES HAQSNSKLNE DQLKRLHMIL KPFMLRRVKK HVQKELGDKI
     ELDVYCDLTY RQRAYYANLR NQISIMDLIE KATLGDDNDS GTLMNLVMQF RKVCNHPDLF
     ERADTSSPLA LVRFAETGSF AREGNDVTVG YTTRSVVEYI LPRLLWRDGG RLTKAGSDNP
     SAGFRSRYLG EMMNIWSSTN IRESVDGTDN FSFLRFADTS IAEAEKVGKT DLFARASELA
     QRRNRLANMH VSYDDDEEDN FTPAHALFLI RQRQDRTALS EITSEGALQN LMNVSHVMYE
     DANLPRMDQA ARPGASAPPI EVVCHTSSTQ IERDRVLFNV PMRKALFGPN LDEQKEFVLQ
     KVPVEQLPPA PLLPKPDNER QRFTSITVPS MRQFITNSGK LAKLDELLFK LKAGGHRVLL
     YFQMTRMIDL MEEYLTYRNW KYCRLDGSTK FEDRRDTVHD FQTNPSIFVF LLSTRAGGLG
     INLTSADTVI FYDSDWNPTI DSQAMDRAHR LGQTRQVTVY RLITRGTIEE RIRKRAMQKE
     EVQRVVITGG AGASSGVDFS GRRAPENRNR DIAMWLADDD QAELIERRER ELLESGELDK
     VAKKRGGGKR KKVAKDMGDG GGVSLDEMYH EGEGNFDDNK LSGAATPNVP DSTDAKPGKK
     KKATGKKAKT TKQRLAIADG QMDM