ID   INO80_CRYNB             Reviewed;        1765 AA.
AC   P0CO17; Q55US0; Q5KHM0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=INO80; OrderedLocusNames=CNBD0390;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000019; EAL21342.1; -; Genomic_DNA.
DR   RefSeq; XP_775989.1; XM_770896.1.
DR   AlphaFoldDB; P0CO17; -.
DR   SMR; P0CO17; -.
DR   EnsemblFungi; AAW43182; AAW43182; CND06010.
DR   EnsemblFungi; EAL21342; EAL21342; CNBD0390.
DR   GeneID; 4935414; -.
DR   KEGG; cnb:CNBD0390; -.
DR   VEuPathDB; FungiDB:CNBD0390; -.
DR   HOGENOM; CLU_002244_0_0_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
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; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW   Hydrolase; Nucleotide-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1765
FT                   /note="Chromatin-remodeling ATPase INO80"
FT                   /id="PRO_0000410113"
FT   DOMAIN          629..759
FT                   /note="DBINO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT   DOMAIN          883..1055
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1457..1607
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1680..1723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1740..1765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          702..745
FT                   /evidence="ECO:0000255"
FT   MOTIF           1006..1009
FT                   /note="DEAQ box"
FT   COMPBIAS        15..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         896..903
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1765 AA;  196403 MW;  C5E120034EEC0A86 CRC64;
     MGAMDDRRYS YPPPRTSYVQ PSTHPSPTAS DYRYRSPVLP QHPPTHHSPS SYSASLYGQP
     KEDPAIAYAR MREEMRTAEE ARREAEALEY RRKRDMEFAA RRPGSELMDD PRRIPHSSFP
     RSQMYGPSAD QSRVMPSRNG KDYISEPPSP SELYPTDEDT ERLPIDRYRR DIDVPPLPRQ
     LPPPPSEIGR MADRARSPSA PIAPPLLKVV RKRTKVIRPN DFLVGNEDVW EDGLIRYQSK
     REDEVRAIAQ WAASCQVRNG VGEPSLPQTQ DESIKVRKIN GDIATPTNKK KRKSRKLNLD
     DELLGLASSP PGSPNAAAEA EKSESKHHIY GMNGPIDPAN PPSPSTIVYP SGLTRAEVIA
     KCEAGDVEGL TEDDVKAVQD EMWMREKAAQ AAENGGVLPT NKDGTVRRKP GPAKGWRKIR
     GIDKKKETTP GKAQSTTAGS VAGSVADEEA EADIAALLDD SIAKKGKKVK RRKLEEPGAE
     SPRFADAEDE YNEHRPSDSV LLDEIEDEHS RAGSVGESNA LDTLPAASAP PKKKNSKTKE
     PGVGKGRWTR PTKPEKELVK KAEALASRTS KASLAGPSDD TFGVGPGPAE EVQEEIKHEY
     APNTHDPRGV SENEAKIRHE LVEDLQKQAW SNIVRDVPRI YRVFQGYDQS MKQIAQRRAQ
     ACVRNAFGQR NQKTMQRQSG KVNKEGAAKA KRIVKELAAF WRKNEKDEVI ARKKAEREAL
     ERAKAEEEAR ETKRQSRKLN FLLTQTELYS HFIGKKIKTK EAEAAEGMDV EEEEKRGMEE
     IAIGEDGEPL PDLDYDEDDE ENLRKHAARG AQAAIQAARD KARAFDDSIV GRGAPLPGDD
     TMDGDELNFQ NPSLGENSVT ITQPKMLMAQ LKEYQLKGLT WLGNLYEQGI NGILADEMGL
     GKTIQSISLL AYLAEHHNLW GPFLVIAPAS TLHNWQQELA RFVPRLKALP YWGSPKDRET
     LRKIWSRKNQ TFSEDSPFHI LITSYQLAVQ DEKYLQGMKW QYMILDEAQA IKSSSSARWK
     SLLSLHCRNR LLLTGTPIQN SMHELWALLH FIMPQLFDSH EEFAEWFSKD IESSSGGVTG
     NLKPEQLKRL HMILKPFMLR RVKKHVQKEL GDKIEIDLLV DLSQRQREIY KALRQRVSIT
     DLLATAENNT DNGNPKNMRS LVNLVMQFRK VCNHPDLFER ADVVSPFVFG EFSQSGNLAR
     EGDGMYLPDS ARNAIEVQIP RILWTDGGKL DIPGEQSLAG SDTKILQNLL NIWTPEWINE
     RTKCADAEFG FVKLVGSSPG ETSRSAKSPV LVQLLEGAEK ERRWTEEGRF VDDSEFAASV
     KKGFRVPSVI PVLTQPGQVS LREISRRVWD ESYLSRDDAR CIGDYAIAPI VKPIASNRSF
     LNAQDRILNQ PLAHSTLYGL APSELHDPLA AEQFSRIAPS VPLTGLIPSS ASSQTPVSPL
     HIPPTKRLIV DSAKLARLDS LLRELKAGGH RVLLYFQMTK MMDLIEEYLI FRQYKYLRLD
     GSSPIAERRD MVTSWQTNPD IFVFCLSTRA GGLGINLTAA DTVIFYDHDW NPSSDAQAMD
     RAHRVGQTKQ VTVYRLVARG TIEERILQMA RGKKDIQDVV VGTKSVSDVA KPSEIVSLFM
     DDEELAESVA KRKQAEAHGY IAPTIIPNGR RSQFGDGLVL DDGEGDDGFF NAAAAARANA
     EEEEGLGAEE ESKGKGKAKA AAAVTFPVPG EKRSHKKGMG KKAQAAAAAA ALERVIAGNE
     EPLAASKPPA KKKVKIALGP DGLPL