ID A0A1F7ZYB4_9EURO Unreviewed; 1692 AA.
AC A0A1F7ZYB4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ABOM_006985 {ECO:0000313|EMBL:OGM44440.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM44440.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM44440.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM44440.1}.
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DR EMBL; LYCR01000055; OGM44440.1; -; Genomic_DNA.
DR STRING; 109264.A0A1F7ZYB4; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000179179; 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:OGM44440.1};
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:UP000179179}.
FT DOMAIN 581..706
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 830..1002
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1405..1565
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 651..692
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1692 AA; 190447 MW; 8F5545A68D72C151 CRC64;
MTGAPPYNPQ SPTQQHHYPG YSPPNKSRPF YPNNDQYQQH PPQTPPAFPP PTTMSRSPHY
SHASPLPATL PPLNGSAPPP HPPDPSSQFQ AHSSAGTPQF PLPRPYSGSV LSSNGASPYG
PSTPSHAHPT GRPEGHLQLS PNKDTESSYL GGTGVAGYPS SIMREPKPAS PPKEAKPARA
ADPMSFASIL SGPAEERSPP KRQSPPPETT PAPVTSTPRE ATQLSPPPPA HVPPSHQRVK
EQEQVLPRLE KKPSSEKRRR NAEQDNKARE PLSGISTNGS LEPTKASTQP WAFLNPRKAL
SERETETINK LMVEIDNAEK SDVEAPGFEE EYEQYKLQSK RRALHALKEE GTKRKRRRNV
FLTNLGKSLE KQASAGMDRF RIANEASVIS EVQAKEIQDE KERKKDMQRK RRRENTVRLE
MQKKLEAERK ANKAQDSAEK AKFLREAERA QRKIKTTKRA LEGVTAPEEI GEVTPLAPNL
EGGTTSSFHI GRSSPSRRKS GRAGPVTRPK KSKEQKQAEK DAAEAAYAAM ENDEPLPLAP
KEDPRKESLK KEAKGSRSKE SSPAPLSAYE TKGYNQIYEQ IWRDIARKDI PKVYRIKALS
LSTRQENLRK TAQLASKQSR KWQERTNKSM KDTQARAKRT MREMMSFWKR NEREERDLRR
LAERQEIESA KKAEAEREAN RQRRKLNFLI SQTELYSHFI GRKIKGAEGD SGEGSDETIQ
SGKDQEHAVD LPPSAADAGA KVTNFEDLDF DAEDESALRQ AAMANAQNAV KEAQDRARAF
NDGQDNMAAL DEGELNFQNP TSLGDIEISQ PSMLTAKLKE YQLKGLNWLV NLYEQGINGI
LADEMGLGKT IQSISVMAYL AEVHNIWGPF LVIAPASTLH NWQQEITKFV PDIKVLPYWG
SAKDRKILRK FWDRKHITYT KESEFHVLVT SYQLVVLDAQ YFQKVKWQYM ILDEAQAIKS
SQSSRWKNLL GFHCRNRLLL TGTPIQNNMQ ELWALLHFIM PTLFDSHDEF SEWFSKDIES
HAQSNTKLNE DQLKRLHMIL KPFMLRRVKK HVQQELGDKV EKDVFCDLTY RQRAYYTNLR
NRVSIMDLIE KAAIGDEADS TTLMNLVMQF RKVCNHPDLF ERAETKSPFS VAHFAETASF
VREGQNVDVG YSTRNLIEYP LPRLLCGSDG RVDVAGPGNL QAGFHGKYLA HLMNIFAPEN
IKHSAAHDGT FSFLRFVDTS INEAYEQSHQ GIFERAIRQR GKSNRLSRLN VVYDDDETTM
ASVLSHTMFN IVQRNDQHAI NDVTTEGHMR ELTTVAQSVF EREGLGIIEP CVSPAASAPP
ITVSSSSRAP LNEMNDSLFN VSVRHALFST PSKQLEQQIL ERKLDPIPYS LPPMLPQPIS
IKGRYTHIEV PSMRRFVTDS GKLAKLDELL RELKAGGHRV LLYFQMTRMI DLMEEYLTYR
NYKYCRLDGS TKLEDRRDTV ADFQQRPEIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP
TIDSQAMDRA HRLGQTRQVT VYRLITRGTI EERIRKRALQ KEEVQRVVIS GGAAGGVDFN
TRNRESRTKD IAMWLADDEQ AELIEQKEKE ALDRGEVFGA SKGGKKAAQK RKRDITLDDM
YHEGEGNFDD ASAKPSGAAT PVSTAENLGT PSSTPVPKRG RGRGTGKGTS KRAKTTKERL
RLIDGDGGLG PS
//
