INO80_ASHGO
ID INO80_ASHGO Reviewed; 1414 AA.
AC Q74Z27;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; OrderedLocusNames=AGR379W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 123; 205 AND 544.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016820; AAS54869.2; -; Genomic_DNA.
DR RefSeq; NP_987045.2; NM_212107.2.
DR AlphaFoldDB; Q74Z27; -.
DR SMR; Q74Z27; -.
DR STRING; 33169.AAS54869; -.
DR PRIDE; Q74Z27; -.
DR EnsemblFungi; AAS54869; AAS54869; AGOS_AGR379W.
DR GeneID; 4623349; -.
DR KEGG; ago:AGOS_AGR379W; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; Q74Z27; -.
DR OMA; FWKKNER; -.
DR Proteomes; UP000000591; Chromosome VII.
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..1414
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074318"
FT DOMAIN 429..554
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 667..839
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1244..1398
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 106..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..341
FT /evidence="ECO:0000255"
FT MOTIF 790..793
FT /note="DEAQ box"
FT COMPBIAS 106..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 681..687
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1414 AA; 161209 MW; 7BF05046BF277114 CRC64;
MSLEALLNKE EKGSGAAREA FMRRMNERFN SVCHKDAREQ QYQDWKYLSY QEFELVNEWS
AASRELTVNQ CGQLLSNVKS AQAEWLAYEE FVAGRARLVA EVEAKREREQ EEQEERQPAR
AKTKERARAR GTAKRAVGRK ATKAPAAPAE QEGGVPAARA AAKAPVRAEG AAEPPLKREL
SGAKLEDEGE GEDDDEEEDE DDEDDEDEDE DEDEEEEEEE ELEELEDIQL LDDDNDKDFS
PEGGRSKSSI KLNTKLDINS DIALIQRELL KMAQKHKSAK AKKRKFTSCV VQRYDSDHTR
LEVKVTLKQL HIKRLKRLLN EAKRKRAAEE ALAANEQQGN LAKRRKTAQK QKPAANGAPA
ASSSEDVTVT EAATPVPAKV NGEAPSNESP VAAIPDINPT TGLPTYGMKM TAKEARAIQR
HYDTTYITVW KDMARKDSAK LSRLVQQIQS IRSANFKKTS SLVAREARKW QSRNFRQVKD
FQTRARRGVR EMSSFWKKNE REERELKKRA EREAIEQAKK EEEERESKRQ ARKLNFLLTQ
TELYSHFIGS KIKTNELEGN MADSNLATAP DVSAIDLSKP PTRKNEVHTI DFDNEDDEEL
HRKAAQNASN ALKETREKAK AFDGMSGDDE ELNFQNPTSL GEITIEQPKI LACTLKEYQL
KGLNWLANLY DQGINGILAD EMGLGKTVQS ISVLAHLAER YNIWGPFIVV TPASTLHNWV
NEIQKFVPDF KILPYWGNGN DRKILRRFWD RKHLRYSKDA PFHVMITSYQ MIVSDAAYLQ
KMKWQYMILD EAQAIKSSQS SRWKNLLSFH CRNRLLLTGT PIQNSMQELW ALLHFIMPSL
FDSHDEFNDW FSKDIESHAQ SNTQLNQQQL RRLHMILKPF MLRRIKKNVQ SELGDKIEID
VMCDLTHRQA KLYQVLKSQV SASYDAIENA ASNSSGDDSG NMSLSDSKIM NTVMEFRKVC
NHPDLFERAD VSSPFSFTSF GQTGSIMREG DVIDVQYSSK NPVSFHLPRL IYDDLILPNY
NHDSDMRTKI LNHMMSIFAP ANSPDLCATL SKVAGVEPNS ILRLSQEHIV KRAIDLSAHS
PNVTRSGIFS VVYEDDKSSL SSLDKTLLIN DKSDYLHTIA RTTQNGVLAS LLNIQGNFYE
NEYMNVLRPA YRPAAAAPPI SIHVMGSSNF SIKRDNALFE PYITRSLGII PPELQTRLTE
KENNIFTALP ISELYPAPLN KSFSSYISMP SMDRFITESA KLKKLDELLV RLKAGEHRVL
IYFQMTRMMD LIEEYLTYRQ YKHIRLDGSS KLEDRRDLVH DWQTKSDIFI FLLSTRAGGL
GINLTSADTV IFYDSDWNPT IDSQAMDRAH RLGQTKQVTV YRLLIKGTIE ERMRDRAKQK
EHVQQVVMEG KTKENNVQTI TANGKTLENL PLPL
