ID   DDX52_RAT               Reviewed;         598 AA.
AC   Q99PT0;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX52;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase ROK1-like;
DE            Short=rROK1L;
DE   AltName: Full=DEAD box protein 52;
GN   Name=Ddx52; Synonyms=Rok1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Li W., Suzuki T.;
RT   "Identification of a novel ROK1-like protein in rat brain.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB055628; BAB32441.1; -; mRNA.
DR   RefSeq; NP_445977.1; NM_053525.1.
DR   AlphaFoldDB; Q99PT0; -.
DR   SMR; Q99PT0; -.
DR   STRING; 10116.ENSRNOP00000003600; -.
DR   CarbonylDB; Q99PT0; -.
DR   PaxDb; Q99PT0; -.
DR   PRIDE; Q99PT0; -.
DR   Ensembl; ENSRNOT00000003600; ENSRNOP00000003600; ENSRNOG00000002612.
DR   GeneID; 85432; -.
DR   KEGG; rno:85432; -.
DR   CTD; 11056; -.
DR   RGD; 621743; Ddx52.
DR   eggNOG; KOG0344; Eukaryota.
DR   GeneTree; ENSGT00550000074863; -.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   InParanoid; Q99PT0; -.
DR   OMA; IRAQHRI; -.
DR   OrthoDB; 400908at2759; -.
DR   PhylomeDB; Q99PT0; -.
DR   TreeFam; TF314448; -.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q99PT0; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002612; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q99PT0; RN.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; NAS:RGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; TAS:RGD.
DR   CDD; cd17957; DEADc_DDX52; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044764; DDX52/Rok1_DEADc.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..598
FT                   /note="Probable ATP-dependent RNA helicase DDX52"
FT                   /id="PRO_0000055062"
FT   DOMAIN          197..375
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          386..547
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          59..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           166..194
FT                   /note="Q motif"
FT   MOTIF           319..322
FT                   /note="DEAD box"
FT   COMPBIAS        59..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         210..217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2R4"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2R4"
SQ   SEQUENCE   598 AA;  67240 MW;  B9E818EA6B144425 CRC64;
     MDSYDLFRRL GAGAKFDVKR FSADATRFQV GKRKFGSDSS ETVKGLDFFG NKKSVSDECG
     GLQTQQELQN EETTEGGLLE RSKEPKKKKR KKMTADVPAQ EDLDGTIQWT SSVEAKLQDK
     KANGEKKLTS EKLEHLRKEK INFFRNKHKI HVQGTDLPDP IATFQQLDQE YKISPRLLQN
     ILDAGFQVPT PIQMQAIPVM LHGRELLASA PTGSGKTLAF SIPILMQLKQ PTNKGFRALV
     ISPTRELASQ IHRELIKISE GTGFRIHMIH KAAIAAKKFG PKSSKKFDIL VTTPNRLIYL
     LKQEPPGIDL TSVEWLVVDE SDKLFEDGKT GFRDQLASIF LACTSPKVRR AMFSATFAYD
     VEQWCKLNLD NIVSVSIGAR NSAVETVEQE LLFVGSETGK LLAMRELVKK GFNPPVLVFV
     QSIERAKELF HELIYEGINV DVIHAERTQQ QRDNTVHSFR AGKIWVLICT ALLARGIDFK
     GVNLVINYDF PTSSVEYIHR IGRTGRAGNR GKAVTFFTED DKPLLRSVAN VIQQAGCPVP
     EYIKGFQKLL SKQKKKMIKK PLERESISTT PKYFLEQAKQ KKVAGQNSKK KETLKGKS