INO80_ASPFU
ID INO80_ASPFU Reviewed; 1708 AA.
AC Q4WTV7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=AFUA_5G06260;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000003; EAL91969.1; -; Genomic_DNA.
DR RefSeq; XP_754007.1; XM_748914.1.
DR AlphaFoldDB; Q4WTV7; -.
DR SMR; Q4WTV7; -.
DR STRING; 746128.CADAFUBP00005266; -.
DR PRIDE; Q4WTV7; -.
DR EnsemblFungi; EAL91969; EAL91969; AFUA_5G06260.
DR GeneID; 3511543; -.
DR KEGG; afm:AFUA_5G06260; -.
DR VEuPathDB; FungiDB:Afu5g06260; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR InParanoid; Q4WTV7; -.
DR OMA; DDMYHEG; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
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; IBA:GO_Central.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; IBA:GO_Central.
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_0000074319"
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 408..581
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..747
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..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..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 408..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; 192291 MW; DDE2B7F271CE1893 CRC64;
MTGAPPYNPQ SPTQQPRFPV YSPPNKNRSY YPNNDQYQQH APQTPPAFAP QPSLSRSPHY
SHAPSPLPAT LPPLNGGAPP PGHHPEPSSQ YQTHSSAGTP QFSLPRPYSA SMMSSNGASS
YNHSTASHAH PSARLESLSQ SPPKKETEPL YPIGGNGAPG YSSSMMREPR PASPPRETKH
ARAADPMSFA SILSGPTEET SPIKQPSLPE ALPGPATTIT PAPPTLAPVP ARRRLTPPPV
THALPPTSQL KVKEPEPISP AALPRLEKKP SAEKRRRNVE QEPKSAEALP VASTHGAFEP
TKAARVSNRK TLTERDAEAI NKIIAEIDNA DKSDVESPGF EVEYGRYMVK SKKRALDAEK
AEGIRRKRRR HDFLVKLGKT FEKQANAGVD RFRAANEASV IAEVQAKEIQ DEKERKKDMQ
RKRRRENTVR LEMQKKLEAE RKANKANDAA EKAKFLREAE RAQRKIKSTK RALEGVTSPE
EIGEVTPLAP NLEGGTTSSF HIGRSSPSRR KSGRSGTSRP KKSKEQKQAE KDAAEAAYAA
MENDEPLPLA PKEDPRKETV KKEAKGARSK ETTPAPVSAF ESKGYNQIYE QIWRDIARKD
IPKVYRIKTL SLSTRQENLR KTAQLASKQS RKWQERTNKS MKDTQARAKR TMREMMSFWK
RNEREERDLR RLAEKQEIES AKKAEAEREA NRQKRKLNFL ISQTELYSHF IGRKIKGAGA
DSSGDTAVDG SDETIQPGKA DHTIDLPPTV ADVGAKVTNF EDLDFDAEDE TALRQAALAN
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 YTNLRNRVSI MDLIEKAAVG DEADSTTLMN LVMQFRKVCN HPDLFERAET
KSPFSVGYFA ETASFVREGQ NVDVRYSTRN LIEYNLPRLL CSPSGRIDMA GPGNEHAGFR
GKYLQHLMNI FTPENIKRSI DEDGAFSFLR FADTSINEAY EQSHLGVFER AVRRRGQSNR
LSHLNVIYDD EEDEKTSKFV LPHSLFNIVQ RNDRQAVRNV TVEGYMRDLM NVSEATFERD
GLGVIEPSAS PAASAPPITI SCSGQVALRE TQDTFFNVSV 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
GNGKGSSKRA KTTTERLRLI DGDGGLES
