ID A0A0E0JIV8_ORYPU Unreviewed; 1110 AA.
AC A0A0E0JIV8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Chromatin-remodeling complex ATPase {ECO:0000313|EnsemblPlants:OPUNC01G16280.1};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC01G16280.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC01G16280.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC01G16280.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR AlphaFoldDB; A0A0E0JIV8; -.
DR STRING; 4537.A0A0E0JIV8; -.
DR EnsemblPlants; OPUNC01G16280.1; OPUNC01G16280.1; OPUNC01G16280.
DR Gramene; OPUNC01G16280.1; OPUNC01G16280.1; OPUNC01G16280.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR OMA; QMASFNS; -.
DR Proteomes; UP000026962; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT DOMAIN 246..411
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 539..690
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 880..932
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 127873 MW; 089314AA7FBA41B4 CRC64;
MAKPVKYDEE EEVSSSGEEE EEQSDGAGSG SGGEEDEEEE EAPAAAAAGE AAGGEEEEVD
EEEIEAVTTG AGADEEEEDG GAAAAAPEEG DEESQSTEDD EAVAGEDDDG DEAEDHAGGA
VVGKREKARL KEMQKLKKQK IQEILDTQNA AVDADMNNKG KGRLKYLLQQ TEIFAHFAKG
NQSKEKKPRG RGRHASKMTE EEEDEEYLKE EEDALAGSGG TRLLSQPSCI KGKMRDYQLA
GLNWLIRLYE NGINGILADE MGLGKTLQTI SLLGYLHEFR GITGPHMVVA PKSTLGNWIK
EIQRFCPILR AVKFLGNPEE RNHIRENLLQ PGKFDVCVTS FEMAIKEKTT LKRFSWRYII
IDEAHRIKNE NSLLSKTMRI YNTNYRLLIT GTPLQNNLHE LWSLLNFLLP EIFSSAETFD
EWFQISGEND QQEVVQQLHK VLRPFLLRRL KSDVEKGLPP KKETILKVGM SQMQKQYYRA
LLQKDLEVIN AGGERKRLLN IAMQLRKCCN HPYLFQGAEP GPPYTTGEHL VENAGKMVLL
DKLLPKLKDR DSRVLIFSQM TRLLDILEDY LMYRGYQYCR IDGNTGGEDR DASIEAFNKP
DSEKFVFLLS TRAGGLGINL ATADVVVLYD SDWNPQADLQ AQDRAHRIGQ KKEVQVFRFC
TEYTIEEKVI ERAYKKLALD ALVIQQGRLA EQKTVNKDDL LQMVRFGAEM VFSSKDSTIT
DEDIDRIIAK GEETTAELDA KMKKFTEDAI KFKMDDTAEL YDFDDDKEEN KLDFKKLVSD
NWIEPPRRER KRNYSESEYF KQALRQGAPA KPREPRIPRM PHLHDFQFFN NQRLNELYEK
EVRYLMQANQ KKDTIDGEDE DQLEPLTAEE QEEKEQLLEE GFATWTRRDF NTFIRACEKY
GRNDIRSIAA EMEGKTEEEV QRYAKVFKER YKELSDYDRI IKNIERGEAR ISRKDEIMRA
IGKKLDRYKN PWLELKIQYG QNKGKFYNEE CDRFMLCMVH KLGYGNWDEL KAAFRMSPLF
RFDWFVKSRT TQELARRCDT LIRLVEKENQ EYDEQERQAR KDKRMAKNMT PTKRSALRVS
EGETTPSNSF KRRRQSLMDD YVGSGRRKRG
//
