ID A0A0E0A5X8_9ORYZ Unreviewed; 1324 AA.
AC A0A0E0A5X8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G05590.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G05590.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G05590.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR STRING; 40148.A0A0E0A5X8; -.
DR EnsemblPlants; OGLUM06G05590.1; OGLUM06G05590.1; OGLUM06G05590.
DR Gramene; OGLUM06G05590.1; OGLUM06G05590.1; OGLUM06G05590.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_31_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
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; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
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; PTHR45623:SF17; CHD3-TYPE CHROMATIN-REMODELING FACTOR CHR7-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 72..155
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 165..225
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 261..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 575..735
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 845..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 801..828
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 152350 MW; CF2AD0FB06BEFE26 CRC64;
MSSLVERLRV RSEKRPLYTL DESDDDLPPR GGGGKGRDRH SDGPTERIER EDAKEDACQK
CGENDNLVSP LTEMEKILDC EETKPDASEE TSSSESGSKK KPVKRYLIKW KGISHLHCTW
VSESEYLETA KIYPRLKTRL NNFHKQMDST DKSDDDYSAI RPEWTTVDRI LATRKSSTGE
REYYVKWKEL TYDECTWEND SDIAVFQPQI ERFNEIQSRR KKSTDKCKSV TREIRQYKES
PKFLSGGTLH PYQLEGLNFL RYSWYHNKRV ILGDEMGLGK TIQSIAFLGS LFVDKLGPHL
VVAPLSTLRN WEREFATWAP QMNVVMYFGS AASREIIRKY EFYYPKEKPK KLKKKKSSPS
NEDKKQSRIK FDVLLTSYEM INMDSTVLKT IEWECMIVDE GHRLKNKDSK LFGQLKEYHT
KHRVLLTGTP VQNNLDELFM LMHFLEGDSF GSIADLQEEF KDINQDKQVE KLHGMLKPHL
LRRFKKDVMK ELPPKKELIL RVELTSKQKE YYKAILTKNY EVLTRRSGGH VSLINVVMEL
RKLCCHAFMT DEPEEPANSE EALRRLLESS GKMELLDKMM VKLKEQGHRV LIYSQFQHML
DLLEDYLSYR KWSYERIDGK IGGAERQIRI DRFNAKNSTR FCFLLSTRAG GLGINLATAD
TVIIYDSDWN PHADLQAMAR AHRLGQTSKV MIYRLVSRGT IEERMMQLTK KKMVLEHLVV
GRLTKGTNIV QEELDDIIRH GSKELFDDEN DEAGKSCQIH YDDAAIDRLL DRDQADGEEP
VEDEEEDEFL KGFKVANFEY IDEAKALAAK EEEARKKAEA EAANSDRANF WDKLLKDRYD
VQKVEEHTTM GKGKRSRKQM AAADEDDITG LHDMSSEDDD YSYDDDVSDN DTSLQSGLAG
RRGPYSKKKQ RSNVDSLPFM EGEGRALRVY GFNQIQRTQF LQTLMRYGFQ NYDWKEFTPR
LKGKSVEEIQ RYAELVMIHL LEDINDSGYY ADGVPKEMRT DETLVRLANI SLVEEKVAAM
EQGKITKLFP SYLLYEFPSL VGGRVWKAEQ DLLLLKALIK HGYARWQYIS DDRDNGIFEA
ARQELRLPTA NELISSHSNN ETNGNLESTQ EGQSNPTSMI HYRDTQRKIV EFIRKRYHLL
ERCLNLEYAV IKTKTPVPDD LAEQDFPGGH RPAVPDYSEM LRELPVLEPI SKEVAPEGTT
DQSQVSHLYN KMCFVLEDSA VPALHSHFGD KAASSGLANS LHKFEAVCED VSRILRSHEN
GTTPKEEVML DASSKETTSP KDPATEVPSS ASKEATPPVQ DPVIEAVKEE PPTVKAEDKM
EIDS
//
