ID B9R9L5_RICCO Unreviewed; 690 AA.
AC B9R9L5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=RCOM_1498590 {ECO:0000313|EMBL:EEF51492.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000256|ARBA:ARBA00006517}.
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DR EMBL; EQ973773; EEF51492.1; -; Genomic_DNA.
DR RefSeq; XP_002510890.1; XM_002510844.2.
DR AlphaFoldDB; B9R9L5; -.
DR STRING; 3988.B9R9L5; -.
DR GeneID; 8266011; -.
DR KEGG; rcu:8266011; -.
DR eggNOG; KOG0331; Eukaryota.
DR InParanoid; B9R9L5; -.
DR OrthoDB; 1188at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12937; GUCT_RH7_like; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.30.70.2280; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 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 SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT DOMAIN 136..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 347..489
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 16..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 75166 MW; 7E5F505BC150D134 CRC64;
MPSIAIANNA ADLKEKKMKK RISLETSEQP EEEIILSDKK EKKMKKDKKK RKAVDSELDE
EDKSETSSEL VEPVNLKTKK KNKKAKIADE NEDGEVETAE EDHPNAISKY RISESLREKL
KSKGIQSLFP IQAMTFDDIL DGSDLVGRAR TGQGKTLAFV LPILESITNG HAKESRKTGY
GRPPSVLVLL PTRELASQVF DDFKVYGESL GLTSCCLYGG ASYHPQEMSL KRGVDIVVGT
PGRVKDHIER GNINLSYLKF RVLDEADEML RMGFVEDVEL ILGKVEDVSK VQTLLFSATL
PEWVKQISSR FLKASKKTID LVGNEKMKAS TNVRHIILPC SASAIPQVIP DIIRCYSSGG
RTIIFTEKRE SANELAGLLH GARALHGEIQ QSQREVTLSG FRSGKFLTLV ATNVAARGLD
INDVQLIIQC EPPRDVEAYI HRSGRTGRAG NTGVAVMLYD PRRSNISKIE RESGVKFEHI
TAPQPADIAQ AVGAVAAEKI TQVSDSIVPA FKSAAEDLLN SSGLSAVELL AKALANAAGY
TEIKSRSLLS SMENHVTLLL EAGRPIYTPS FAFGVLRRFL PEDKVESVKG MTLTADGKGA
VFDVAAADID TFLAGQDNAA NVSLEILKAL PPLQEKDQSR GRFGGGGRGR GGFSDRNGGG
RFSGGRGGRG GDRRNDRFGG GRGRNNGSRW
//
