ID   DDX51_DANRE             Reviewed;         652 AA.
AC   Q6DRI7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=ATP-dependent RNA helicase DDX51;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 51;
GN   Name=ddx51;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA   Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA   Hopkins N.;
RT   "Identification of 315 genes essential for early zebrafish development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits. {ECO:0000250}.
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   -!- 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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY648772; AAT68090.1; -; mRNA.
DR   RefSeq; NP_001003864.1; NM_001003864.1.
DR   AlphaFoldDB; Q6DRI7; -.
DR   SMR; Q6DRI7; -.
DR   STRING; 7955.ENSDARP00000029445; -.
DR   PaxDb; Q6DRI7; -.
DR   PRIDE; Q6DRI7; -.
DR   GeneID; 445387; -.
DR   KEGG; dre:445387; -.
DR   CTD; 317781; -.
DR   ZFIN; ZDB-GENE-040927-28; ddx51.
DR   eggNOG; KOG0350; Eukaryota.
DR   InParanoid; Q6DRI7; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q6DRI7; -.
DR   PRO; PR:Q6DRI7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 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   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; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..652
FT                   /note="ATP-dependent RNA helicase DDX51"
FT                   /id="PRO_0000228098"
FT   DOMAIN          234..442
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          480..626
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           212..220
FT                   /note="Q motif"
FT   MOTIF           362..365
FT                   /note="DEAD box"
FT   COMPBIAS        9..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   652 AA;  72460 MW;  27B9AE89032F020A CRC64;
     MALFTINRYL GEEEEEDSEK QSRSKALLAK LQKQVKARGQ QSVSNTPKEE EEQQDDKEHK
     KRKHKLQETK GKIKKSESVQ NTDPTEEADS SVKKKKKRKK SLSTEDVIVK IEENESENEK
     SVDITGPTPS SPVQFKAEKA EELTSSSQSN YQVLGGFKEK DVQKVKRVLP QWLSQPDVIQ
     KDIKSNLIPI SEVPGICPTL LRKLQTNGIQ SFFPVQAEVI PAILESVGSG LLVGPGGYRP
     RDVCVSAPTG SGKTLAFVIP VVQALSKRVV RQVRALAVLP TKELAQQVSN VFSAYTEGSS
     LKVVMITGQK SFAAEQTALS EIRGGVSHSM ADIVVATPGR LVDHINKNSS FSLQHLRFLI
     IDEADRMIDS MHQSWLSQVT KAVYSTPGET HTSVFRRTVP GPITAASLSP PQIPLQKLLF
     SATLTQNPEK LQLLDLHQPR LFSSTHSLTD NPAQSQDTFH FPQGLSEYYV PCTFSKKPLI
     ILHFLLRLKF SPALCFTNSR EGAHRLYLLV KLFGGVEVAE FSSKLSPGER QKTLKDFEKG
     KIPLLISTDA AARGIDINGV KCVINYDAPQ YIRTYIHRVG RTARAGKAGL AFTFLLKVQE
     KRFLKMVSDA GSPGIQKQHV HPEALKSMES RYEQVLAELG TIVKEENEKK RF