ID   INO80_COCIM             Reviewed;        1662 AA.
AC   Q1DUF9; J3K7T6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=INO80; ORFNames=CIMG_06054;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704912; EAS30575.3; -; Genomic_DNA.
DR   RefSeq; XP_001242158.1; XM_001242157.2.
DR   AlphaFoldDB; Q1DUF9; -.
DR   SMR; Q1DUF9; -.
DR   STRING; 246410.Q1DUF9; -.
DR   PRIDE; Q1DUF9; -.
DR   EnsemblFungi; EAS30575; EAS30575; CIMG_06054.
DR   GeneID; 4561120; -.
DR   KEGG; cim:CIMG_06054; -.
DR   VEuPathDB; FungiDB:CIMG_06054; -.
DR   InParanoid; Q1DUF9; -.
DR   OMA; DDMYHEG; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000001261; 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; -; 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..1662
FT                   /note="Chromatin-remodeling ATPase INO80"
FT                   /id="PRO_0000350958"
FT   DOMAIN          558..683
FT                   /note="DBINO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT   DOMAIN          808..980
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1384..1544
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1574..1662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          356..439
FT                   /evidence="ECO:0000255"
FT   COILED          581..671
FT                   /evidence="ECO:0000255"
FT   MOTIF           931..934
FT                   /note="DEAQ box"
FT   COMPBIAS        13..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..51
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..206
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1589..1608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1645..1662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         821..828
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1662 AA;  187850 MW;  397D69D7F19956C0 CRC64;
     MAGVPPYGMH SPTQQPRYPS YSPSTRDRQP YSGNDPYQHP PRTPPSFAPP SSLSRSPHFA
     RPPSPMNTTL PPLNGTVVNA DGSPPYHGHS GSATSGYTLP RPFGGSLMSA TSHSPPPSYS
     HASGSHSHPS NIPDSFSQSP KRESEPYDVR SDRTGPVSQT PARPASPKES KSARSNPMSF
     ANILSGPADE PPPRRSSPPP QTYKSSTLPP IAPTPKVDKE PLSEPEKRRG SSHYETAYNE
     MPHRPAMNGF TPAKSPLAAM PSPLSKSRKL VDEEEIDKIS RENIARALEQ IDALDNSDVE
     APGFEQEWER YMAKSRKRAR ELDAIEGRKR KRRRTEFLGK LAKMFEKQAL QGIERFNRIH
     EAEVQMEVQQ KEIQEEKERK KDMQRKRRRE NTVRHEMEKL NAAQKKANKI EDEAEKQKLA
     KEIARSKKKI KDTTLALERG EASQEISEVN PLAPNLEGGT TSSFHIRTKS PPPPKKRAAK
     GTSSRPRKSK EKKQAEKDAA EAAYAAMENE DLVPLAPKED PRKTSLKKES KAARSKEPSP
     VPATPYDSKG YNQFYEQLWR DIARKDIPKV YRIKVVSLST RQENLRKTAQ LAAKQARKWQ
     EKTNRSMKDT QARAKRTMRE MMTFWRRNER EERDMRRLAQ RQELELAKKA EADREANRQR
     RKLNFLISQT ELYSHFIGRK IKTDKAQDSG DATTTAAIEG NGEGKVPDSL VPLPDGGAKV
     TSFDDLDFDA EDETALRQAA MANAQSAVQE AQDRARAFNG EENKMADFDE GEMNFQNPTS
     LGDVEVSQPK MLTCQLKEYQ LKGLNWLVNL YEQGINGILA DEMGLGKTVQ SISVMAYLAE
     VHDIWGPFLV VAPSSTLHNW QQEIVKFVPD LKVLPYWGSA KDRKVLRKFW DRRNITYRKQ
     SEFHVLVTSY QLVVGDAQYF QKIKWQYMIL DEAQAIKSSQ SSRWKSLLGM HCRNRLLLTG
     TPIQNNMQEL WALLHFIMPT LFDSHDEFSE WFSKDIESHA QSNTKLNEDQ LKRLHMILKP
     FMLRRIKKHV QKELGDKVEK DVFCDLTYRQ RAYYTSLRNR VSIMDLIEKA AIGDDTDSTT
     LMNLVMQFRK VCNHPDLFER AETTSPFSVC YFAETASFVR EGPFVDVGYS TRNLVEYDLP
     RLLCSPEGRL DVAGPGNNKA GFEGRYLSHL MNIWTPENIR ESMSHNDAFS WLRFADTSVG
     EAYEVSHKGV FERAVRRRDY STRLSLLDVA YDAEDGVNIN SVHVHSLFNI VERNDRRALA
     DITATGYMRE LLNVASNVAE RGGIRTIEPC AKPGASAPPI TISCSGQAAI AEARATFFNT
     AVRHALFAAP TKAMEEEILS NKLDPAPYSL RPLLPQPGSM KGRYTNITVP SMRRFVTDSG
     KLAKLDELLR ELKNGGHRVL LYFQMTRMID LMEEYLTYRN YKYCRLDGST KLEDRRDTVS
     DFQQRPEIFV FLLSTRAGGL GINLTAADTV IFYDSDWNPT IDSQAMDRAH RLGQTKQVTV
     YRLITRGTIE ERIRKRALQK EEVQRVVISG GAAGGVDFNA RSRENRTKDI AMWLADDEQA
     EILEQKEKEA LEKGEELGAK KGRKAAGKRK RDITLDDMYH EGEGHFEDNS TKPSGAATPV
     SGDVSGVPGV KGRRGRGGGG VGRSKKAKTM KERLRLVDGE VD