ID W9J6U4_FUSOX Unreviewed; 1864 AA.
AC W9J6U4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|ARBA:ARBA00019805, ECO:0000256|RuleBase:RU368001};
DE EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
GN ORFNames=FOYG_00412 {ECO:0000313|EMBL:EWZ00582.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWZ00582.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWZ00582.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair.
CC {ECO:0000256|RuleBase:RU368001}.
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:0000256|RuleBase:RU368001};
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368001}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025, ECO:0000256|RuleBase:RU368001}.
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DR EMBL; JH717839; EWZ00582.1; -; Genomic_DNA.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368001};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU368001};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU368001};
KW DNA-binding {ECO:0000256|RuleBase:RU368001};
KW Helicase {ECO:0000313|EMBL:EWZ00582.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753}.
FT DOMAIN 812..937
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 1060..1232
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1633..1792
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 882..923
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1838..1854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 211269 MW; 9B86B4E7C4935991 CRC64;
MDQNGYNSSV LQRPPHREDG GDDDRDSRPH HHHHHHHHHH HHNNRRDGDS AGPGPIVGET
ATASSNAGSA NVHQHSTFSL RSPKSEYRPP PFTSPNGHSH SHSHSHQNTP SAGHSLQSPP
RPALPNPYMS SSTGAPGGPV APSLPPPVGL NSSSPGSSAA GLHQQQHHRQ PPAPPPAGPP
PVSPLHPPVA YYPPGSNHDI YIPRETKPAS RGFYDPTTDT TKESRVSDAA TPGASWHNAN
ANANAPPVGT PKTRDPYPYS QSAEQSTPSY YNGSYTSPRD PSYSRPRSPV SHSHQNPPAG
SLSPPGRQPL LASPSARHGA TANMTSSTNG GSTLTPYKSD LAAPSPPKPA SASTSRANPM
SFDSILSSSE PARKPKEQSP LISREVEPEI KQERDSRRDR EPKHDSREPK QTKRSLEPEA
DHDTEVEKDV ETELEPFPGR DKEREPPVKK RGGRKSTKGR ASDIRDAATP KNGRRLSIKK
ESPTPRLPAK RQANGLLKPK TWSAEMEKKI QNAETQIDNR ASNLEPDEFD QQQYKERAQK
RRRVMDQLDL EHGLSRRAAF ATSTGKKLVL HAELGKRRYD DVFYDEALHE VREQEVYAEK
ERKKDMQRKR RREKSMAVTM EQKEAALARA EAAEDETERQ KHLRDAERAS KKAQQTKLIL
QKGIKGPARN LELNLEGGTM SSFQASDVES GEAGTPSGKR KGKGRSGPRL KKSKEQKQAE
KDSAEAAQAA LDAGEELPTK EENRVRIKIK KSKKDPSAET EKDKDDGDKT EDEPVEKKSK
KSKDKDKEKV DDIPDNEKRF MSKGYNQIYD QIWRDMARKD VNKTFKLAVD SYATKASNLK
KTAILASKEA KRWQLRTNKG TKDLQARAKR VMRDMMGFWK RNEREERDLR KAAEKQEIEN
ARKEEADREA ARQKRKLNFL ISQTELYSHF IGKKIKTDEV ERSTDNPDVA KDAHQIDQQK
LDIDEPTGPV TGKVTNFENL DFEEGSEEAL RAAAMANAQN AIAEAQKKAR DFNNQGLDMD
EEGEMNFQNP TGLGDVEIEQ PKLINAQLKE YQLKGLNWLV NLYEQGINGI LADEMGLGKT
VQSISVMAYL AEKHDIWGPF LVVAPASTLH NWQQEIAKFV PEFKILPYWG GANDRKVLRK
FWDRKHTTYR KDAPFHVCVT SYQLVVSDVA YFQKMRWQYM ILDEAQAIKS SQSSRWKALL
NFHCRNRLLL TGTPIQNNMQ ELWALLHFIM PSLFDSHDEF SEWFSKDIES HAQSNTKLNE
DQLKRLHMIL KPFMLRRVKK HVQKELGDKI EMDIFCDLTY RQRAYYSNLR NQINIMDLVE
KATMGDDQDS GTLMNLVMQF RKVCNHPDLF ERAEVNSPFA CAYFAETASF VREGSEVAVG
YSSRNLIEYE LPRLIWRKGG RINKAGPDSQ VAGWKNQALN HMMNVWSPDN IRESCDGSKA
FSWLRFADTS PYEAYEATHQ SLIVRAAKEL QKRDRLGYMN VAYSDIEDQN YTPAHALFQI
RARQNRKPLA DITSEGILTQ LMNVAQSDYN ESGLGRLEPA GRPRASAPPI QVSCRSWGSE
AERSEALFNA PIRKILYGPT VFEEKALVEK KLPMELWPTR EMLPKPDHEK KGFTNISVPS
MRRFVTDSGK LAKLDELLFK LKSEGHRVLL YFQMTRMIDM MEEYLTYRNY KYCRLDGSTK
LEDRRDTVHD FQTRPEIFIF LLSTRAGGLG INLTSADTVI FYDSDWNPTI DSQAMDRAHR
LGQTKQVTVY RLITRGTIEE RIRKRAMQKE EVQRVVIQGG GASVDFSGRR APENRNRDIA
MWLADDEQAE MIERREKELL ESGELEKQQK KKGGKRRKAE NTASLDEMYH EGEHNSPIKS
LILS
//
