ID A0A2I4G6V8_JUGRE Unreviewed; 1516 AA.
AC A0A2I4G6V8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 30.
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 Name=LOC109005253 {ECO:0000313|RefSeq:XP_018839629.2};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018839629.2};
RN [1] {ECO:0000313|RefSeq:XP_018839629.2}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018839629.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_018839629.2; XM_018984084.2.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000235220; Chromosome 3.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000235220}.
FT DOMAIN 332..457
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 574..745
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1186..1336
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1516 AA; 173289 MW; 6963506BC01C0D38 CRC64;
MNFQLPQQDD DFDYYGNSSQ DESRGSQGGT IMNHGNGPMR ERESIKRRKQ SGNSDDEDEE
SYYGTRVTED RYRSMLGEHV QKYKRRRVKD SSASPAPTRM GVPLPTSNLG SKARKLGNEH
RGGFNEVETI SDWLNDINRQ KQENYHETDF APLNGSERTT YEPAFLDIGD GITYKIPPTY
DKSAASLNLP SFSDFQVEDF YLKGTLDLGS LAAMMANNKR LGPRSWAGMG EPQLQYESLH
ARLKALSASK LPHKFSLKVS DIGLHSFIPE GAAGNIKRSI LSEGGVLQVY YVKVLEKGDT
YEIIERALPK KTKLKKDPSV IEEEEKEKIG KVWVNIVRRD IPKHHRIFTA FHRKQLIDAK
RFSENCQREV KMKVSRSLKL MRGAAIRTRK LARDMLLYWK RVDKEMAEVR KREEREAAEA
LRREQELREA KRQQQRLNFL IQQTELYSHF MQKKSNSQPS EALPVGGEKL NDQELVLSSS
DAEPDEEEDP EEAELKKEAF RAAQDAVSKQ KKLTSTFDSE CSRLRQAAES EVAGASNIDL
HNPSTMPVTS TVQTPRMFKG FLREYQLKGL QWLVNCYEQG LNGILADEMG LGKTIQAMAF
LAHLAEEKNI WGPFLVVAPA SVLNNWNDEV SRFCPDMKTL PYWGGLQDRT ILRKRIKPKD
LYRREAGFHI LITSYQLLVS DEKYFRRVKW QYMVLDEAQA IKSSNSIRWK TLLSFNCRNR
LLLTGTPIQN NMAELWALLH FIMPTLFDSH EQFNEWFSKG IESHAEHGGT LNEHQLNRLH
SILKPFMLRR VKTDVVSELT SKTEVTVHCK LSSRQQAFYQ AIKNKISLAE LFDGNRGHLN
EKKILNLMNI VIQLRKVCNH PELFERNEGS TYLHFGKIPN SLLPPPFGEL EDIHYAGAHN
PITYKIPKLV HLESAHSSET LCLEVGRAVS RESYQKHFNM FSPENVYRSI FLPEDNLNGL
SVRSGTFGFT RLMDLSPSEV TFLASGSFME QLLFSVMRWD RKFLDGIIDL LMEKMDDDPE
CSYLKKGDMR AVTRMLLMPS RSETNLLRSK YATGPGDAPF EALVIPHQDR LLYNSRLLHS
AYTFIPRIRA PPIDAHCSDR NFAYKMSEEL HDPWIKRLFT GFARTSEFNG PRKPDGRPHN
LIQEIDSELP VSQPALQLTY KIFGSSPPIR SFDPAKLLTD SGKLQTLDLL LKRLRAENHR
VLLFAQMTKM LNILEDYMNY RKYRYLRLDG SSTITDRRDM VRDFQHRSDI FVFLLSTRAG
GLGINLTAAD TVIFYESDWN PTLDLQAMDR AHRLGQTKDV TVYRLICKET VEEKILQRAS
QKNTVQQLVM MGGHVQGDLL APEDVVSLLL DDAQLEQKLR EIPLQVKDRQ KKKNSTKGIL
LDAEGDASLE DLTNVESQGT GYEPSPDPER AKSSNKKRKA ASDKQALPRS MNSQKMTLAM
DDELDDSLQN PDLQAQRPKR PKRPTKSVNE TLEPSFTGTP TGVSEQTHYP STSELGSGVF
RPEAEQDISK HGDSFT
//
