INO80_GIBZE
ID INO80_GIBZE Reviewed; 1904 AA.
AC Q4IL82; A0A098D5N1; A0A0E0RSM9; V6QYI0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN Name=INO80; ORFNames=FGRRES_02026, FGSG_02026;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; DS231663; ESU07413.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF74254.1; -; Genomic_DNA.
DR RefSeq; XP_011317898.1; XM_011319596.1.
DR AlphaFoldDB; Q4IL82; -.
DR SMR; Q4IL82; -.
DR STRING; 5518.FGSG_02026P0; -.
DR PRIDE; Q4IL82; -.
DR EnsemblFungi; ESU07413; ESU07413; FGSG_02026.
DR GeneID; 23549425; -.
DR KEGG; fgr:FGSG_02026; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G04893; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_26_1_1; -.
DR InParanoid; Q4IL82; -.
DR Proteomes; UP000070720; Chromosome 1.
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; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1904
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074325"
FT DOMAIN 809..934
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 1057..1229
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1630..1789
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..655
FT /evidence="ECO:0000255"
FT COILED 706..783
FT /evidence="ECO:0000255"
FT COILED 877..922
FT /evidence="ECO:0000255"
FT MOTIF 1180..1183
FT /note="DEAQ box"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1070..1077
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1904 AA; 215076 MW; 33323FB578CE30E0 CRC64;
MDQNGYNSSA LQRPPRRGDE GCEEDRDSRP HHHHRHHHHH HHHRRDGDLP AGAVAGEAAT
ASSNAGGANA HQHSTFSLRS PKPEYRPPPF SSPNGHNHSH HNTSTSSANH SLQSPPRPAL
PNPYMSSSTG APGGPVAPAL PPPVGINSSS SPGSSAAGLH QRHHQPGAPA HQHRAAPPPV
SPLHPPVAYY PPGTNTDIYI PPPEPKPASR GFYDPTTDTT KERRISDAAT PGASWHNANA
NAPPAGTPKT RDPYSYSQTA DQHTPSYYNG GSYTSPRGPS YNRPRSPLSH SHQNPPAGSL
SPPGQQPLLA SPSVRHGTTA NMNPTTNGAS AIPPFKSDLA APSPPKPAPS STTSRANPMS
FDSILSSSEP APKPKEPSPI IAREPEIKEE REPRRDRESK RDSREPKQTK RSLEPELDHD
TEVEKDVETE PEPLPSREKE KEPAPKKRGA RKSTKGRASD IRDAATPKNG RRLSVKKESP
TPRLPAKRQA NGQPKPKTWS AEMEKKIQNA ESDIENRAAN LDADEFDEQQ YKERAQKRRR
VMSELDVEYG LSRRDALANT ISKKLVLHAE LGKRRYDDVF YDEALHEVRE QEVYAEKERK
KDMQRKRRRE KSMAVTMEQK EAALARAEAA EDETERQKHL RDAERASKKA QQTKLILQKG
IKGPARNLEI NLEGGTMSSF QASDVESGEA GTPSGKRKGK GRSGPRLKKS KEQKQAEKDS
AEAAQAALDA GEELPTKEEN RVRIKIKKTK KDVAVDSEKD KDEAEKTEEE VVEKKTKKSK
DKDKEKVDDI PDNEKRFMSK GYNQIYDQIW RDMARKDVNK TFKLAVDSYA TKASNLKKTA
ILASKEAKRW QLRTNKGTKD LQARAKRVMR DMMGFWKRNE REERDLRKAA EKQEIENARK
EEADREAARQ KRKLNFLISQ TELYSHFIGK KIKTDEVERS TDNPEIAKDA HQTDQKMLDI
DEPTGPVIGK VTNFENLDFE EGSDEALRAA AMANAQNAIA EAQKKARDFN NQGLDMDDEG
EMNFQNPTGL GDVEIEQPKL INAQLKEYQL KGLNWLVNLY EQGINGILAD EMGLGKTVQS
ISVMAYLAEK HDIWGPFLVV APASTLHNWQ QEIAKFVPEF KILPYWGGAS DRKVLRKFWD
RKHTTYRKDA PFHVCVTSYQ LVVSDVAYFQ KMRWQYMILD EAQAIKSSQS SRWKALLNFH
CRNRLLLTGT PIQNNMQELW ALLHFIMPSL FDSHDEFSEW FSKDIESHAQ SNTKLNEDQL
KRLHMILKPF MLRRVKKHVQ KELGDKIELD IFCDLTYRQR AYYSNLRNQI NIMDLVEKAT
MGDDQDSGTL MNLVMQFRKV CNHPDLFERA EVNSPFACAY FAETASFVRE GNDVAVGYSS
RNLIEYELPR LVWRDGGRVH KAGPDSQVAG WKNRTLNHLM NIWSPDNIRD SSDGSKAFSW
LRFADTSPNE AYQATHQSLI ARAAKELQKR DRLGYMNVAY SDTEDANFTP AHALFQIRPR
QNRKPLADIT NEGILSRLMN VAQGDYDESG LGRLEPAGRP RASAPPIQVS CRSWASEFER
SEVLFNAPIR KILYGPTVFE EKALVEKKLP MELWPTRQML PKPDHEKKGF TNISIPSMQR
FVTDSGKLAK LDDLLFKLKS EGHRVLLYFQ MTRMIDMMEE YLTYRNYKYC RLDGSTKLED
RRDTVHDFQT RPEIFIFLLS TRAGGLGINL TTADTVIFYD SDWNPTIDSQ AMDRAHRLGQ
TKQVTVYRLI TRGTIEERIR KRAMQKEEVQ RVVIQGGGAS VDFSGRRAPE NRNRDIAMWL
ADDEQAEMIE RREKELLESG ELEKQQKKKG GKRRKAENSA SLDEMYHEGE GNFDDGSKGV
SGTATPATAA TPADSDSKGK KGRKGTKRAK TAKQRLAIAD GMME
