ID INO80_DEBHA Reviewed; 1364 AA.
AC Q6BGY8; B5RUY3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; OrderedLocusNames=DEHA2G22682g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382139; CAR66027.1; -; Genomic_DNA.
DR RefSeq; XP_002770708.1; XM_002770662.1.
DR AlphaFoldDB; Q6BGY8; -.
DR SMR; Q6BGY8; -.
DR STRING; 284592.Q6BGY8; -.
DR GeneID; 8999286; -.
DR KEGG; dha:DEHA2G22682g; -.
DR VEuPathDB; FungiDB:DEHA2G22682g; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; Q6BGY8; -.
DR OMA; FWKKNER; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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:RHEA.
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:DNA-templated transcription; IEA:InterPro.
DR CDD; cd18002; DEXQc_INO80; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR031047; DEXQc_INO80.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; CHROMATIN-REMODELING ATPASE INO80; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 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; P-loop containing nucleoside triphosphate hydrolases; 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..1364
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074323"
FT DOMAIN 335..460
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 579..751
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1146..1302
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 702..705
FT /note="DEAQ box"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 592..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1364 AA; 155935 MW; 872B6BCD8E7CBC68 CRC64;
MNISSMLSND SNTASQDVGG NFDDSQRNND KGGSQDANSK KMGTGEAEDH ANGNASVEGN
GIANHGSATN GNTKGTDDSS NVNIVESIIP KPIRPTRSSI ESDEEDVGKN YNSIISNDSE
HISQRYLENF EDKVNAINKI DQVLIKGNNM RVLNQEEENL NILIRNSGEI AENYIDRVVT
EDISSKANIL NGKDSVGKEF KWGSTRDMKK RELELEVDNA SKADTAAKKG GNKSKQGATK
STPAKKAKAK PKRKPSATDD TSEESQLGKK RKTRAGSVSG ASQNDEKSAN GKVKLKLTLK
DQAEEDSASA DAASKVTTKE QKIITKQYDN TFVSIWKDLS RKDGPKVSRL MQQSTQAKMI
NLKKTSILAA REAKRWQLKN NRNQKDLTTK ARRAMREMFN FWKRNERIER ELRKKHEKEI
LDKAKKEEEE RESKRQSRKL NFLITQTELY SHFIGKKIKT DEFEGTDSDP NANFKSANHH
YDKYSNIDGE GKDFNSIDFD NEDEESLNKA AAVNAQIALE AAKTKAQAFD NDPLKNPDTN
GEEMNFQNPT LLGDINISQP DLLKCTLKEY QVKGLNWLAN LYEQGINGIL ADEMGLGKTV
QSISVLAYLA ETHNIWGPFL VVTPASTLHN WQQEISRFVP EFKVIPYWGN AKDRKVLRKF
WDRKNFRYGK DAPFHVLVTS YQLVVADAAY FQKMKWQYMI LDEAQAIKSS QSSRWKSLLS
FSCRNRLLLT GTPIQNSMQE LWALLHFIMP SLFDSHDEFS DWFSKDIESH AQSNTELNEQ
QLRRLHVILK PFMLRRIKKN VQSELGDKLE IDVFCDLTHR QKKYYQMLTS QISIMDLLDS
ANNSSDDSAQ SLMNLVMQFR KVCNHPDLFE RADVKSSFAF GRFAETSSFL RETNELEMSY
STENLIKYNM PRIVYEEILQ PTFDNDVGSR KKINNMFNIY HPSNIANDEL ENFSWLRFVD
QSPQEMNNLS KQNIIERAIN NREYSDINYE RINRLKYTYD EDNESFLPNS KLLLINELQN
NHALISNSTY LKELYSIKKK VYEDMVINNM KPAAEPLVKA PPVAVVCDNI SFVHDLQDSL
FDPKIRSSLM PLPFNRELEL LKSSIPITEY PKSNMLPNAI NKFIDYSNIR MPSMNRFITE
SGKLSKLDEL LVDLRQNDHR VLIYFQMTKM MDLMEEYLTY RQHKYIRLDG SSKLDDRRDL
VHDWQTKPEI FVFLLSTRAG GLGINLTAAD TVIFYDSDWN PTIDSQAMDR AHRLGQTRQV
TVYRLLTRGT IEERMRDRAK QKEQVQQVVM EGKSAIANKE ESGNKKKDVA FLLLGNDDSS
AAALNDDSEE KQNLQDSKKS QAKNLEDMYH EGEGEFSGNV TPSL
//
