ID   DDX55_DANRE             Reviewed;         593 AA.
AC   Q8JHJ2; Q6PBZ0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP-dependent RNA helicase DDX55;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 55;
GN   Name=ddx55;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Embryo;
RX   PubMed=12006978; DOI=10.1038/ng896;
RA   Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA   Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA   Hopkins N.;
RT   "Insertional mutagenesis in zebrafish rapidly identifies genes essential
RT   for early vertebrate development.";
RL   Nat. Genet. 31:135-140(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-489.
RC   TISSUE=Retina;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable ATP-binding RNA helicase. Plays an essential role in
CC       early embryonic development. {ECO:0000269|PubMed:12006978}.
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   -!- 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   -!- DISRUPTION PHENOTYPE: Embryos have bent ceratohyal cartilage.
CC       {ECO:0000269|PubMed:12006978}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF506203; AAM34647.1; -; mRNA.
DR   EMBL; BC059534; AAH59534.1; ALT_TERM; mRNA.
DR   AlphaFoldDB; Q8JHJ2; -.
DR   SMR; Q8JHJ2; -.
DR   STRING; 7955.ENSDARP00000020323; -.
DR   PaxDb; Q8JHJ2; -.
DR   ZFIN; ZDB-GENE-021212-1; ddx55.
DR   eggNOG; KOG0345; Eukaryota.
DR   InParanoid; Q8JHJ2; -.
DR   PhylomeDB; Q8JHJ2; -.
DR   PRO; PR:Q8JHJ2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005730; C:nucleolus; 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   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Developmental protein; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..593
FT                   /note="ATP-dependent RNA helicase DDX55"
FT                   /id="PRO_0000252213"
FT   DOMAIN          40..223
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          241..405
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          524..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          535..565
FT                   /evidence="ECO:0000255"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT   MOTIF           171..174
FT                   /note="DEAD box"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        8
FT                   /note="K -> G (in Ref. 1; AAM34647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="A -> S (in Ref. 2; AAH59534)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   593 AA;  66911 MW;  07697AB5E5FB53D7 CRC64;
     MENITDGKWG SLPVKLHDNI LQTLKELGFT YMTPVQSACI PLFMSNKDVA AEAVTGSGKT
     LAFVIPALEI LLKREEKLKK MQVGALIITP TRELAMQISE VMGRFLQGFP QFTQILLIGG
     SNPIEDVEKL KTQGANIIIA TPGRLEDMFR RKADGLDLAT AVKSLDVLVL DEADRLLDMG
     FEASLNTILG YLPKQRRTGL FSATQTQELE KLVRAGLRNP VRITVKEKGV AASSVQKTPA
     KLSNYYTMCR AEEKFNTLVA FLRQHKHEKQ LVFFSTCACV EYFGKALEVL VKNVSIHCIH
     GKMKHKRNKI FADFRALKSG ILVCTDVMAR GIDIPEVNWV LQYDPPSSAS SFVHRCGRTA
     RIGNQGNALV FLLPMEESYV NFLSINQKCP LQSFSSVKDV VDVLPKLKAM ALGDRAMFEK
     GMRAFVSYVQ AYAKHECSLI FRIKDLDFAA LARGFALLRL PKMPELRGKT FPDFKAEAID
     TDTIRFKDKN REKQRQKWLA EQKEKEVPLR KNFIKNKAWS KQKIKKDRKK KRLPKAKLDQ
     DSDAAEEDLN ELMNDTRLLK KLKKGKITEE DFDKQMSSTD KHKPAGIDSS DGD