ID A0A059DH76_EUCGR Unreviewed; 1533 AA.
AC A0A059DH76;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=EUGRSUZ_A02310 {ECO:0000313|EMBL:KCW90118.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW90118.1};
RN [1] {ECO:0000313|EMBL:KCW90118.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW90118.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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; KK198753; KCW90118.1; -; Genomic_DNA.
DR STRING; 71139.A0A059DH76; -.
DR EnsemblPlants; KCW90118; KCW90118; EUGRSUZ_A02310.
DR Gramene; KCW90118; KCW90118; EUGRSUZ_A02310.
DR eggNOG; KOG0388; Eukaryota.
DR InParanoid; A0A059DH76; -.
DR OMA; FWKKNER; -.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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}.
FT DOMAIN 345..477
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 601..772
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1213..1363
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 30..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..463
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 175083 MW; 4B936BEC66DEDF33 CRC64;
MDPRRHSKDS LSYSSLFNLE PLMSYKLPQR DDDFDYYGSS SQDESRGSQG AALRPSNGTM
SNKKKKRSFN SDNEDGDGYY GAKITEDRYR AMLGEHIQKY RRRPKDHSSF AQLATVGIPL
PRGNNSGPKT HKLANERRGG LYDVEAEPEW ANGINLHKDR NNQNTDVAPV NSLERVVYEP
SFLDIADGIT YKIPPTYDTL AASLNLPSFS DVTVEEFHLK GSLDLGSLAK LMASEKRLGP
RNRAGMGELR PQYESLHARL KASNAAQQFS LKVSDVGLSS IPEGAAGNIK RSILSEGGVL
QVYYVKVLEK GDAYEIIERS LPKKAKVIKD PSLIEKEEME KIGKVWVNIV RRDIPKHHRI
FTAFHRKQLN EAKRFSENCQ REVKMKVSRS LKLMRGAAIR TRKLARDMLL FWKRVDKEMV
WHILFPAEVR KREEREAAEA LKREQELREA KRQQQRLNFL IQQTELYSHF MQNKPNSQQP
EAFPVGDTKV NDQETLLSSL DMEPGQDEDP EEVELRKEAL KAAQDAVSKQ KRLTDAFDTE
CLRLRHPSET ELTMPDTLVT GSSNIDLQTP STMPAMSTVR TPELFRGSLK EYQLKGLQWL
VNCYEQGLNG ILADEMGLGK TIQAMAFLAH LAEEKNIWGP FLVVAPASVL NNWADEISRF
CPDLKTLPYW GGLQERTVLR KNINPKRLYR RDAGFHILIT SYQLLVSDEK YFRRVKWQYM
VLDEAQAIKS SSSIRWRTLL SFNCRNRLLL TGTPIQNNMA ELWALLHFIM PTLFDSHEQF
NEWFSKGIEN HAEHGGTLNE HQLNRLHAIL KPFMLRRVKK DVIQELTRKT EITVHCKLSK
RQQAFYQAIK NKISLTELFD GSRGHLNEKK ILNLMNIVIQ LRKVCNHPEL FERNEGSTYF
HFGEIPNSLL PPPFGELEDV HYSGGQNPIT YQMPKLVNEE SLQHPGMLDA SVRHGLCRES
YQKLFNIFSP SNVHQSTFSE ENSSKGPFVK SGTFGFTHLI DLSPAEVAFV ATGTYMEKLL
FSMGEWNGQL LDQMVDFVIE TTDDDMRCNH LDRGKVKAVT RMLLMPSRSE ASLLTRKYAT
GPSDAPFEAL VYSDQDRFLS NIRLLHSTHA FIPRARAPPI GVHCSNRNFT YKTIEELHHP
RMKRLFLGFA RTSEYNGPRK PHCPPHPLIE EIDAELPISQ PALELTYRIF GSCPPMQSFD
PSKLLTDSGK LQTLDILLKR LRAENHRILL FAQMTKMLNI LEDYMNYRKY RYLRLDGSST
IMDRRDMVRD FQHRNDIFVF LLSTRAGGLG INLTAADTVI FYESDWNPTL DLQAMDRAHR
LGQTKDVTVY RLICKETVEE KILQRASQKN TVQQLVMTGG HVQGDLLAPE DVVSLLLDDA
QLEQKLREIP PQVKDRQRKK QSTKGIRLDA EGDASLEDLT NIAAEGAGNE PTPDADKTKS
SSKKRKATAD KQSSLKSRNP PRMSEHSSSP TEYPFDDSLP YNDQQSQKPK RLKRPKKSVN
ENLEPAFTPA PNIPPEQTQF QPIHEFGSSD PST
//
