INO80_LODEL
ID INO80_LODEL Reviewed; 1575 AA.
AC A5E0W5;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; ORFNames=LELG_03252;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981527; EDK45073.1; -; Genomic_DNA.
DR RefSeq; XP_001525324.1; XM_001525274.1.
DR AlphaFoldDB; A5E0W5; -.
DR SMR; A5E0W5; -.
DR STRING; 379508.A5E0W5; -.
DR PRIDE; A5E0W5; -.
DR EnsemblFungi; EDK45073; EDK45073; LELG_03252.
DR GeneID; 5232539; -.
DR KEGG; lel:LELG_03252; -.
DR VEuPathDB; FungiDB:LELG_03252; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_20_1_1; -.
DR InParanoid; A5E0W5; -.
DR OMA; GCQREVK; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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:InterPro.
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:transcription, DNA-templated; IEA:InterPro.
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..1575
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000350959"
FT DOMAIN 505..630
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 749..921
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1315..1470
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 872..875
FT /note="DEAQ box"
FT COMPBIAS 86..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 762..769
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1575 AA; 177637 MW; 200B11A10F765839 CRC64;
MNILSMLSND SAVQLQLQLQ LQLQLQLNLQ SAPSKASPPT LLPKQTTATT TNATGNTKTV
ARYSAGDINI LNDENSHGVD ESIDEPVTNG QATNKESVKQ EPTQPTNNTE TEKKPLTLSI
QNGADKKSLP PQSQPPRINP LVADVTLSTS KFKNVLAHIQ HDQLEIDLDY KFKFESNVSL
IDQLDKNQRL SQDLRILKFD EVKSNNYLIS THQFTTNYID RVVAEDISSR NNKISDTNKN
KEIIHIDHSK PLHHNSTRGK EYKWGSTREI HKVESKPKRK RNTENSETNN SRSTVSSKAS
TPSKSLAFGS THHVPIRPKG SKGTNLSSSS GPITDITNDS NNVRRSSRPK SKRKAYEDGE
GEDNGNNIDS NSTDNNNRNK TQEGGRGPKR IRIKLKVKPE GENEGEEKDE GKGKGRGKGK
GKGKGKGKEK DGDKEEEDEN NANGENGKSK GSVSSSTTTT TTAAAAAAGG GGSTGSALGT
TTSNSSTSKE QKAFMRQYDN TYVAIWKDMS RKDGPKVSRL MQQSTQAKLI NLKKTCILAA
REAKRWQVKN TKNQKDLSTK ARRAMREMFN FWKRNERIER ELKKKHEKEL VEKAKREEEE
RESKRQSRKL NFLITQTELY SHFIGKKIKT DEIEGTDADP RIKAQEKAHL DKYAGVDAAN
NDILAIDFDN DDEDALHRAA AQNAQNALAN AQNQAKQFDD TEPFKNPDTN GEEMNFQNPT
LLGDLSIEQP KMLKCTLKEY QIKGLNWLAN LYEQGINGIL ADEMGLGKTV QSISVLSYLA
ETHNIWGPFL VVTPASTLHN WQQEISKFVP NFKVLPYWGH AKDRKVLRKF WDRKSLRYDK
DAPFHVLVTS YQLIVSDIAY FQKMKWQYMI LDEAQAIKSS QSSRWKSLLS LSCRNRLLLT
GTPIQNSMQE LWALLHFIMP TLFDSHDEFS DWFSKDIESH AQSNTGLDEQ QLRRLHMILK
PFMLRRIKKN VQSELGDKVE IDLFCDLTNR QKKYYQSLRS QISIMDLIDA TTTNSSSNNS
SLDDSSTTSL VNLVMQFRKV CNHPDLFERA DVRSPMALVK FAETGSFLRE GNDLDVSYAS
ENLINYNLPR LIYDDLISAN ENKNDFGSVY AKFSVYDPEN LRDLGWISSA GTSPNEIQQL
GKMNVLERAI KLQRYTTGSP LDRINYLYEG DYSSPNSKLL INPQNQHMIS QQQIENSSVL
LDLCNISQKV YEEMYLNTQD PAFTPLASAP PITIVCSSNN FQNKLQNELF NPTIRSALAP
MSLNKELEFM NNNTPLELYP PSNMLPSSLS KVNDYSNIRM PSMDRFITES GKLAKLDELL
VKLKQEDHRV LIYFQMTKMM DLMEEYLTFK QHKYIRLDGS SKLDDRRDLV HDWQTKPEIF
VFLLSTRAGG LGINLTAADT VVFYDSDWNP TIDSQAMDRA HRLGQTRQVT VYRLLTRNTI
EERMRDRAKQ KEQVQQVVME GKATTIMSKK EDAASKKKDV AFLLLGGSGD GDGDGTGVNS
GVDTSNDVSK STTPKPEVGK KKNNGNKKNV FGNGKKRVRE EDGEEEDALN SKRLQELYHE
GEGEFSGTVT PAPGV
