INO80_KLULA
ID INO80_KLULA Reviewed; 1489 AA.
AC Q6CNY4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, 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; OrderedLocusNames=KLLA0E08965g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99442.1; -; Genomic_DNA.
DR RefSeq; XP_454355.1; XM_454355.1.
DR AlphaFoldDB; Q6CNY4; -.
DR SMR; Q6CNY4; -.
DR STRING; 28985.XP_454355.1; -.
DR PRIDE; Q6CNY4; -.
DR EnsemblFungi; CAG99442; CAG99442; KLLA0_E08999g.
DR GeneID; 2893796; -.
DR KEGG; kla:KLLA0_E08999g; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; Q6CNY4; -.
DR OMA; FWKKNER; -.
DR Proteomes; UP000000598; Chromosome E.
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; -; 2.
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; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1489
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074326"
FT DOMAIN 518..643
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 758..930
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1323..1479
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 112..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 881..884
FT /note="DEAQ box"
FT COMPBIAS 112..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..371
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 771..778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1489 AA; 170981 MW; 9F8BE0231A158F87 CRC64;
MSLEKLLNRE ENDSSKRTDF MGRWYLKMSK ICERDDREMD YQNWKFLSYQ EFELINEWNQ
QGKELTKDNC ERLLVNMDKT HKEWVEYQKF KEQKDAIIAE LKESIQIIKQ EPSIPSGADA
NSVVSSDTEQ IQDSETTANS KKSPAINGIK TSGKSPTKSP ATNGRRRGAG GNRRVKRPSN
LSKTVRSRNA TDGDENGNEN IENGGTTPKR RSRPKKILVS NVSKDVDAEE EDDIHTEKDA
SGSAADLDKD IVDESINDSE NAPRKRPVSS TSLLSRNKSN KPTKSSPLTP DSAREKENVN
GVTEGNEDMD HDSVLDADDS AIGSDDNPND EQEEADDENV DEEAEDENDE AEVEDDIDDL
GAPEDDGDDD FAPSYSAISK VKVNKKVNID SPMPAIQKEL RKMAIKSSVA KAMKRKFTNC
KVISYSPESQ LEIKITLKQL HIRKYKRHLA EEERKRKAEE ALIKAEEEAK KRKLAPPPPP
PPQQVRRVEH DLPTYGMKIT LKEARAIQRH YDQTYITIWK DMARRDSGRI SRQLQQIQSI
RGQNFRKTSS LCAKEARRWQ MRNFRQVKDF QTRARRGIRE MSSFWKKNER EEREMKKKAE
KEAIEQAKKE EEQRENLRAA KKLNFLLTQT ELYSHFIGSK IKTNELEGTM TDDSLTSMSN
NKNKVVDLTK TAASKTNVES IDFATEDDEK LRLMAAQNAS NALKETQDKA RKFDEEDEED
GELNFQNPTS LGEITIDQPK MLACTLKEYQ LKGLNWLANL YDQGINGILA DEMGLGKTVQ
SISVLAHLAD RYNIWGPFIV VTPASTLHNW VNEISRFVPQ FKILPYWGNA NDRKTLRKFW
DRKHLRYGRD APFHVMVTSY QMVVSDASYL QKMKWQYMIL DEAQAIKSSQ SSRWKTLLSF
HCRNRLLLTG TPIQNNMQEL WALLHFIMPS LFDSHDEFSD WFSKDIESHA ESNTELNQEQ
LRRLHMVLKP FMLRRIKKNV QSELGDKIEI DVLCDLTFRQ AKLYQVLKSQ VSGGYDAIEN
AAGNDDVTSD QKLVNLVMEF RKVCNHPDLF ERADVMSPFS FVSFGESASL SREGDFVEVN
YSAKNLINYN LPRLIYDELV VPNYNNDVDV RAKLLYHTMN IFHPANSFQL CFILSKLTDT
SPNKFATLLE QNVINRAIDL QNDGYFNTAK YSIAYDEGEK IFSSNLLIND KLKYLHLLKN
STSGSVLKNL LEIPSSVYEN EYFNSISPAY HPAASAPPIN IDVLASNNFV QKKQYEMFNP
SISSALSSIP SSVQHKLIVE KGIPIEELPV TEMAPKAFNN SFTSYIEMPS MDRFITESAK
LKKLDELLVK LKEEDHRVLI YFQMTKMMDL MEEYLTYRQY THIRLDGSSK LDDRRDLVHD
WQTKPDIFIF LLSTRAGGLG INLTAADTVI FYDSDWNPTI DSQAMDRAHR LGQTRQVTVY
RLLIRGTIEE RMRDRAKQKE HVQQVVMEGK AKENKQKIIE VEKEHSESA
