ID A0A0E0AAD7_9ORYZ Unreviewed; 927 AA.
AC A0A0E0AAD7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
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:OGLUM06G18040.2};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G18040.2}
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:OGLUM06G18040.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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; EC=3.6.4.13;
CC Evidence={ECO:0000256|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
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DR AlphaFoldDB; A0A0E0AAD7; -.
DR STRING; 40148.A0A0E0AAD7; -.
DR EnsemblPlants; OGLUM06G18040.2; OGLUM06G18040.2; OGLUM06G18040.
DR Gramene; OGLUM06G18040.2; OGLUM06G18040.2; OGLUM06G18040.
DR eggNOG; KOG0342; Eukaryota.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17964; DEADc_MSS116; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF715; DEAD-BOX ATP-DEPENDENT RNA HELICASE 31; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 436..464
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 467..650
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 684..835
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 436..464
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 124..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 101560 MW; D54FF435F2C6BEDE CRC64;
MRRHHHLLGL LRRATASPTP ASRRAGPPLP GLLQDPLRNG AAAAGPRFFS SRAGPGAGAA
AKSLIEDEAE LSDWISDLKT DSFHLGLSSG DEGEASTRGP AASRGGRRGR DSRGPPPRSR
FGGGDFGGDR RGFERRGRMV SNNELGDDDD DEDEVGFGSA RGRRDRGGRQ SEFSYGGRRG
NDFDDDGGGF RSTRGQRGRG GRLANVSRRG YDFDDEPGFQ SPKGQRGQGG RYSDLDDDEG
GFGSPRGRRG RGGRMSGVSR RGGRGSDLDD SEDDEYSRGS SPRGRRGRGG RMSGVSRKGG
RGSDLDDSED DENDSIDSRG RRRDHGTRGR NVGSLGPRRG GRGGDADFSD RRSRGGKMFD
FGLSEDDSEL GEVDEDDGPS GFEDDLFDDE GGEKDLVKSP AKNSAPFESI KGEPVDQEGV
VHTRESGGGD SYLSQTRFDE CSLSPLTLKG VKAAGYERMT AVQEATLPII LKGKDVLAKA
KTGTGKTVAF LLPAIEVVSK LPPIDRDQKR PPISVVVVCP TRELADQAAA EANKLLKFHP
SIGVQLVIGG TRMALEQKRM HTNPCQILVA TPGRLKDHME NTPGFATRLM GVKVLILDEA
DRLLDMGFRT DIERIVAALP KQRQTLLFSA TVPDEVRQVC HIAMKRDLEF VNTVEEGSEE
THSQVKQMHV VAPLDKQFSI LYGLLTDHIS ENVDYKVIVF CTTAKVTSLV AELLSELKLN
VREIHSRKPQ SYRTRISKEF KESKGLILVS SDVSARGVDY PNVTLVVQMG VPTDREQYIH
RLGRTGRRGN EGSGILLLAP WEEYFLRSIK DLPITEATLP LIDLDTKRKV EKALAHVEVK
DKELAYQAWL GYYNSNKFIG RDKYQLVSLA NEFSRSLGLN NPPAVPKLVL RKMGLNNIPV
YATTLGTLYK VKVRRQNMQE ALSIHYL
//
