ID J3LNT2_ORYBR Unreviewed; 1499 AA.
AC J3LNT2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=102700789 {ECO:0000313|EnsemblPlants:OB03G27080.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G27080.1};
RN [1] {ECO:0000313|EnsemblPlants:OB03G27080.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G27080.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB03G27080.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) 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_015690894.1; XM_015835408.1.
DR STRING; 4533.J3LNT2; -.
DR EnsemblPlants; OB03G27080.1; OB03G27080.1; OB03G27080.
DR GeneID; 102700789; -.
DR Gramene; OB03G27080.1; OB03G27080.1; OB03G27080.
DR KEGG; obr:102700789; -.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_20_2_1; -.
DR OMA; FWKKNER; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000006038; 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; 2.
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:UP000006038}.
FT DOMAIN 346..471
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 579..748
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 39..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..457
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 48..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 170817 MW; 3F15EB03FCE2E0AB CRC64;
MDPRRPPPRG GANGGGLSYS TLFNLEPLLN FKVPLPEDLD RHRRRSPNGS MSSQGQGSLS
DQYNGISDAS HGLNRKRKHH LDGASDDDDT DAYSNQITEE HYRTMLSEHV QKYRRSKFKE
DVFGSDPPQA IVPRKHKNGT ARVTKCRSDT RNVATLGGAE ATAEYNGMKY INAHGGFNKL
VASLDSSYLD MGDNVSYIIP EGYDKLAPSL NLPVFSDIRV EENFLNSTLD LRTLAAMLST
DQKFETTNRG GLAEPQPQYE SLQERVKVQK FALQVTEDPF AIPEGAAGRI RRFIISESGS
LDVHYVKVLE KGDTYEIIER SLPKKQIVRK DPSEIAREDS EKTIKLWHAI AVKGIPRHHR
NFMALLKKRQ VDAKRFSDNC QREVKLKVSR SLKLMRGAAI RTRRLARDML IFWKRVDKEQ
YELRKREERE AAEALKREEE LREAKRQQQR LNFLLSQTEL YSHFMQNKAS ESASPDEGSV
PEPDEEDPEE AELKREALRA AQHAVSQQKR MTNAFDSEIG RLHQSSDSGI ATDDLSTVEP
NKIDLLHPST MPEKSSVQTP ELFKGALKEY QLKGLQWLVN CYEQGLNGIL ADEMGLGKTV
QAMAFLAHLA EDKNIWGPFL VVAPASVVNN WAEEVIRFCP DLKILPYWGP ERMVLRKNIN
PKRLYRRDAS FHILITNYQI LVNEEKLLRR VKWQYMVLDE AQAIKSSSSQ RWKTLLSFNC
RNRLLLTGTP IQNNMAELWA LLHFIMPTLF DSHEQFNEWF SKGIEGHAEH GGALNEHQLS
RLHAILKPFM LRRVKIDVIA EMTKKKEEIV PCRLSSRQQV FYQAIKNKIS LNELLDGSRG
SLNDKKLLSL MNIVMQLRKV CNHPELFERN EGSSYFYFAD IPNSLLSPAF GELQDVHYAG
KRNPIMFEIP KLVYEGIISN MEMTLHGCGF PCGSFNRMFN IFSTSYIHQS AFPEAISPKN
AVLSSGAFGF TRLINLSPLE TSFLATCSSF HRLVFSAVRW NKKYMDELVD AFLDSESTDL
DSTHNDVTKV RAVARLLLSP TKADSSLLRT KMETGPSDSP YETLVLSHHE RLVSNIRLLR
STYAFIPPAR APPINVWCAD RNFAYKLTDE MHDPWAKKLF VGFARTSEFN GPREPISPHP
LIQELHTDLP CPEPMLQLPY RIFGSSPPMS NFDPAKMLTD SGKLQTLDTL LRRLRAENHR
VLLFAQMTKM LDILEDYMNF RKFKYFRLDG SSAISDRRDM VRDFQNRNDV FVFLLSTRAG
GLGINLTAAD TVIFYEIDWN PTQDQQAMDR THRLGQTKEV TVYRLICKDT IEEKILQRAK
QKNAVQELVM KGKHVQDDHL MRQEDVVSLL IDDTQMSHKL KEISMQAKDR QKKRRSKGIK
VDNEGDLMLE ELDDPTTGAA EQDNTSSKKR KSSQKKLSKS QGNDSVDKNV EAEGVGEAED
EDNIAAPRPK RSKRLMKNVN DDKESEPTTD GDNLADPAEN DISRDDDDTA EAQDQTPSA
//
