ID   DDX55_XENLA             Reviewed;         594 AA.
AC   Q6AZV7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable ATP-binding RNA helicase.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC077172; AAH77172.1; -; mRNA.
DR   RefSeq; NP_001086608.1; NM_001093139.1.
DR   AlphaFoldDB; Q6AZV7; -.
DR   SMR; Q6AZV7; -.
DR   BioGRID; 103303; 1.
DR   IntAct; Q6AZV7; 1.
DR   PRIDE; Q6AZV7; -.
DR   DNASU; 446443; -.
DR   GeneID; 446443; -.
DR   KEGG; xla:446443; -.
DR   CTD; 446443; -.
DR   Xenbase; XB-GENE-972465; ddx55.S.
DR   OMA; DRAIHDK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 446443; Expressed in egg cell and 19 other tissues.
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   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; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..594
FT                   /note="ATP-dependent RNA helicase DDX55"
FT                   /id="PRO_0000252214"
FT   DOMAIN          40..223
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          254..411
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          502..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          486..542
FT                   /evidence="ECO:0000255"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT   MOTIF           171..174
FT                   /note="DEAD box"
FT   COMPBIAS        502..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..533
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   594 AA;  67560 MW;  E0BFA268637967EA CRC64;
     MENVTEGTWD SLPQKLNGSI RRTLEELKFT HMTPVQSATI PLFMNNKDIA AEAITGSGKT
     LAFVIPLLEI LLKREEKLKK NQVGALIITP TRELAVQIDE VLSCFTKHFP QFSQILLIGG
     SNPVDDVRKF KEHGGNIIVA TPGRLEDMFR RQADGLDLVI CVKTLDVLIL DEADRLLDMG
     FEASINTILG FLPKQRRTGL FSATQTQELE NLVRAGLRNP VRIAVKEKGV AATSTQKTPI
     RLQNYYMICK ADEKFNKLIA FLQKRKQEKH LVFFSTCACV EYYGKALEML LKPVKVMCIH
     GKMKHKRNRI FTEFRKINSG ILVCTDVMAR GIDIHEVNWV VQYDPPSSAS AFVHRCGRTA
     RIGHHGSALV FLLPMEESYV SFLSINQKCP LQEMTELIIS VDLLPKLKAM AETDRAVFEK
     GMKAFVSYVQ AYAKHECNLI FRVKDLDFSS LARGFGLLRM PRMPELKGKN FSDFVSTLID
     TDSIAYKDKN REKQRQKMLK ERKEKLETEG RKHFAKNKAW SKQKARKEKK QKVALKRKKE
     EGSDIDEGDV DELLQDTRLL KRLKKGKITE EEFEKQLTAV GGKSEVEEGS EDSN