INO80_NEOFI
ID INO80_NEOFI Reviewed; 1708 AA.
AC A1CZE5;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
DE AltName: Full=Putative DNA helicase ino80;
DE EC=3.6.4.12;
GN Name=ino80; ORFNames=NFIA_036870;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; EC=3.6.4.12;
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; DS027686; EAW24115.1; -; Genomic_DNA.
DR RefSeq; XP_001266012.1; XM_001266011.1.
DR AlphaFoldDB; A1CZE5; -.
DR SMR; A1CZE5; -.
DR STRING; 36630.CADNFIAP00003391; -.
DR EnsemblFungi; EAW24115; EAW24115; NFIA_036870.
DR GeneID; 4592352; -.
DR KEGG; nfi:NFIA_036870; -.
DR VEuPathDB; FungiDB:NFIA_036870; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR OMA; DDMYHEG; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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..1708
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350961"
FT DOMAIN 592..717
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 845..1017
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1422..1582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..478
FT /evidence="ECO:0000255"
FT COILED 634..706
FT /evidence="ECO:0000255"
FT MOTIF 968..971
FT /note="DEAQ box"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1689..1708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 858..865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1708 AA; 192150 MW; BF15656B6402394E CRC64;
MTGAPPYNPQ SPTQQPRFPV YSPPNKNRSY YPNNDQYQQH PPQTPPAFAP QPSLSRSPHY
SHAPSPLPAT LPPLNGGAPP PGHHSEPSSQ YQAHSSAGTP QFSLPRPYSA SMMSSNGASP
YNHSTSSHAH PSARLESLSQ SPPKKETEPL YPIGGNGAPG YSSSMMREPR PASPPRETKH
ARAADPMSFA SILSGPTEES SPKKQPSLPE ALPAPATTIT PPPPALAPVP ARRRLTPPPV
THGLPPTSQL KVKEPEPISP AALPRLEKKP GAEKRRRNAE QEPKSAEALP VASANGAFEP
TKAARVSNRK TLTERDAETI NKIIAEIDNA DKSDVESPGF EAEYDGYIVK SKKRALDAEK
AEGIRRKRRR HDFLVKLGKT FEKQANAGVD RFRAANEASV IAEVQAKEIQ DEKERKKDMQ
RKRRRENTVR LEMQKKLEAE RKANKANDAA EKAKFLREAE RAQRKIKSTK RALEGVTSPE
EIGEVTPLAP NLEGGTTSSF HIGRSSPSRR KSGRSGTSRP KKSKEQKQAE KDAAEAAYAA
MENDEPLPLA PKEDPRKETL KKEAKGARSK EPTPSPVSTF ESKGYNQIYE QIWRDIARKD
IPKVYRIKTL SLSTRQENLR KTAQLASKQS RKWQERTNKS MKDTQARAKR TMREMMSFWK
RNEREERDLR RLAEKQEIES AKKAEAEREA NRQKRKLNFL ISQTELYSHF IGRKIKGAGA
DSSGDTAVDG SDETIQPGKA DHTIDLPPSV ADVGTKVTNF EDLDFDAEDE TALRQAAMAN
AQNAVKEAQE RARAFNAEEN PMAALDEGEL NFQNPTSLGD IEISQPKMLT AKLKEYQLKG
LNWLVNLYEQ GINGILADEM GLGKTIQSIS VMAYLAEVHN IWGPFLVIAP ASTLHNWQQE
ITKFVPDIKV LPYWGSAKDR KVLRKFWDRK HITYTKESEF HVLVTSYQLV VLDSQYFQKV
KWQYMILDEA QAIKSSQSSR WKNLLGFHCR NRLLLTGTPI QNNMQELWAL LHFIMPTLFD
SHDEFSEWFS KDIESHAQSN TKLNEDQLRR LHMILKPFML RRVKKHVQQE LGDKVEKDVF
CDLTYRQRAY YANLRNRVSI MDLIEKAAVG DEADSTTLMN LVMQFRKVCN HPDLFERAET
KSPFSVGYFA ETASFVREGQ NVDVRYSTRN LIEYSLPRLL CSSSGRVDMA GPGNEQAGFR
GKYLQHLMNI FTPENIKRSI DEDGGFSFLR FADTSINEAY EQSHLGVFER AVRRRGQSNR
LSRLNVIYDD EEDEQTSKSV LPHSLFNIVQ RNDRQAVRNV TVEGYMRDLM NVSEVTFERE
GLDVIEPSAS PAASAPPITI SCSGQVALRE TQDSFFNVSV RHALFSTPSR QMEQQILEKK
LDPAPFSLPP MLPKPISTKG RYTHIEVPSM RRFVTDSGKL AKLDELLREL KAGGHRVLLY
FQMTRMIDLM EEYLTYRNYK YCRLDGSTKL EDRRDTVADF QQRPEIFVFL LSTRAGGLGI
NLTAADTVIF YDSDWNPTID SQAMDRAHRL GQTRQVTVYR LITRGTIEER IRKRALQKEE
VQRVVISGGA AGGVDFNTRN RESRTKDIAM WLADDEQAEL IEQKEKEALD RGEVFGAGKG
GKKAAQKRKK DLTLDDMYHE GEGNFDDISA KPSGAATPVS TADNFGTPSS TPVPKRGRGR
GTGKGSSKRA KTTTERLRLI DGDGGLES
