INO80_ASPCL
ID INO80_ASPCL Reviewed; 1707 AA.
AC A1C9W6;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=ino80; ORFNames=ACLA_009570;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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;
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; DS027049; EAW12534.1; -; Genomic_DNA.
DR RefSeq; XP_001273960.1; XM_001273959.1.
DR AlphaFoldDB; A1C9W6; -.
DR SMR; A1C9W6; -.
DR STRING; 5057.CADACLAP00001450; -.
DR EnsemblFungi; EAW12534; EAW12534; ACLA_009570.
DR GeneID; 4706087; -.
DR KEGG; act:ACLA_009570; -.
DR VEuPathDB; FungiDB:ACLA_009570; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_0_1; -.
DR OMA; DDMYHEG; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000006701; 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..1707
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350954"
FT DOMAIN 593..718
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 847..1019
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1423..1583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..478
FT /evidence="ECO:0000255"
FT COILED 635..706
FT /evidence="ECO:0000255"
FT MOTIF 970..973
FT /note="DEAQ box"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
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..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 860..867
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1707 AA; 191994 MW; 877FE262C23F9D8D CRC64;
MTGGPPYNSQ SPTQQPRYPV YSPPSKTRPY YPNNDQYQQH PPQTPPAFPP QPPLARSPHY
SHAPSPLPAT LPPLNGGAPP SHHQESSSQY QAHQSSGTPQ FPLPRPYSAS VLSSNGASPY
NHPTPSHAHP SSGRLDSLSQ SPPKKDQESL YPIGGNVASG FSSSIMLSPP CILSDSIQKP
ARAADPMSFA SILSGPTEER PLPRKQSPLP EPAPVQTPAP APPVLAPVPA ARKATPPPPT
APVPVPAPLP EIKEPEPLPT PLPRLEKKPS AEKRRRNVDQ ESRASESLPV PPTNGVSEPA
KVSRASNVRK TMSERDTEAI NKIIAEIDNA EKSDVESPGF EAEYERYIAK GKKRALDAEK
AESIRRKRRR HDFLVKLGKT FEKQANAGMD RFRVANEASV IAEVQAKEIQ DEKERKKDMQ
RKRRRENTVR LEMQKKIEAE RKANKANDAA EKAKFLREAE RAQRKIKSTK RALEGVTSPE
EIGEVTPLAP NLEGGTTSSF HIGRSSPSRR KSGRSGGSSR PKKSKEQKQA EKDAAEAAYA
AMENDEPLPL APKEDPRKES LKKEAKGARS KEPTPQPLSA FESKGYNQIY EQIWRDIARK
DIPKVYRIKA LSLSTRQENL RKTAQLASKQ SRKWQERTNK SMKDTQARAK RTMREMMSFW
KRNEREERDL RRLAEKQEIE SAKKAEAERE ANRQRRKLNF LISQTELYSH FIGRKIKGAE
ADASGDAAVD GSDETVRPGK AGDHTIDLPS SVADLSTKVT NFEDLDFDAE DETALRQAAM
ANAQNAVKEA QDRARAFNAE ENPMAALDEG ELNFQNPTSL GDIEISQPNM LTAKLKEYQL
KGLNWLVNLY EQGINGILAD EMGLGKTIQS ISVMAYLAEV HNIWGPFLVI APASTLHNWQ
QEITKFVPDI KVLPYWGSAK DRKVLRKFWD RKHITYTKES EFHVLVTSYQ LVVLDSQYFQ
KVKWQYMILD EAQAIKSSQS SRWKNLLGFS CRNRLLLTGT PIQNNMQELW ALLHFIMPTL
FDSHDEFSEW FSKDIESHAQ SNTKLNEDQL RRLHMILKPF MLRRVKKHVQ QELGDKVEKD
VFCDLTYRQR AYYTNLRNRV SIMDLIEKAA VGDEADSTTL MNLVMQFRKV CNHPDLFERA
ETKSPFSLAH FAETASFVRE GQNVDVRYST RNLIEYDLPR LLFSSSGRLD VAGPDNEKVG
FQNKYLQHLM NIFTPENIKR SVEDDGAFSF LRFADTSINE AYEQSHLGVF ERAVRRRGQS
DRLSQLGVIY DNEGDQTANS VLPHSLFNIV ERNDRQAVYD VAPEGYMRDL MTVSESSFER
QGLNVIEPCA SPAASAPPIF ISCSGQTALR ETNDTFFSVP VRHALYSTPS RQLEEQILEK
KLDPAPFSLP PMLPKPLSAK GRYTHIEVPS MRRFVTDSGK LAKLDELLRE LKAGGHRVLL
YFQMTRMIDL MEEYLTYRNY KYCRLDGSTK LEDRRDTVAD FQQRPDIFVF LLSTRAGGLG
INLTAADTVI FYDSDWNPTI DSQAMDRAHR LGQTRQVTVY RLITRGTIEE RIRKRALQKE
EVQRVVISGG AAGGVDFNTR NRESRTKDIA MWLADDEQAE LIEQKEKEAL DRGEVFGAGK
GGKKAALKRK KDLTLDDMYH EGEGNFDDIS AKPSGAATPV STADNIATPS STPVPKRGRG
RGTVKGSSKR AKTTTERLRL IDGDGGL
