ID   DDX55_CHICK             Reviewed;         591 AA.
AC   Q5ZLN8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=ATP-dependent RNA helicase DDX55;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 55;
GN   Name=DDX55; ORFNames=RCJMB04_5g4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719696; CAG31355.1; -; mRNA.
DR   RefSeq; NP_001006185.1; NM_001006185.1.
DR   AlphaFoldDB; Q5ZLN8; -.
DR   SMR; Q5ZLN8; -.
DR   STRING; 9031.ENSGALP00000005215; -.
DR   PaxDb; Q5ZLN8; -.
DR   GeneID; 416820; -.
DR   KEGG; gga:416820; -.
DR   CTD; 57696; -.
DR   VEuPathDB; HostDB:geneid_416820; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   InParanoid; Q5ZLN8; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q5ZLN8; -.
DR   PRO; PR:Q5ZLN8; -.
DR   Proteomes; UP000000539; 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; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..591
FT                   /note="ATP-dependent RNA helicase DDX55"
FT                   /id="PRO_0000252212"
FT   DOMAIN          40..223
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          254..402
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          482..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..591
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        485..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..535
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   591 AA;  67242 MW;  AB9E2A82987E2AF9 CRC64;
     MEAVTEGGWS SLPVALSPGV LRALQDLGFD RMTPVQSATI PLFMSNKDVA AEAVTGSGKT
     LAFVIPILEI LLRREEKLKK MQVGAIIITP TRELAIQIDE VLTHFTKHFP KFSQILLIGG
     RNPMEDVEKF KEHGGNIIVA TPGRLEDLFR RKADGLDLAS CVKSLDVLVL DEADRLLDMG
     FESSLNAILA FLPKQRRTGL FSATQTQEVE NLVRAGLRNP VRISVKEKGV AATNTQKTPT
     RLENYYMICK ADEKFNQLVH FLRQHKQEKH LVFFSTCACV EYYGKALESL IKQVKIMCIH
     GKMKHKRNKI FTEFRRLAGG ILVCTDVMAR GIDIPEVHWV LQYDPPSSAS AFVHRCGRTA
     RIGNAGSALV FLLPMEESYI NFLSINQKCP MQEMQPQRNV LDLLPKLKSM ALADRAVFEK
     GMKAFVSYIQ AYAKHECNLI FRIKDLDFAS LAKGFALLKM PKMPELRGKC FPDFTPVTVN
     TDSIPFKDKN REKQRQKQLE QQRKEREESE GKKKFIKNKS WSKQKAKREK KRKLTAKRKR
     EEGSDMEDED MEELLNDTRL LKRLKKGKIS EEEFEKRLTG SQSKFKEAAA D