ID   DDX55_CAEBR             Reviewed;         577 AA.
AC   Q61R02; A8X337;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX55 homolog;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 55;
GN   ORFNames=CBG06798;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE601347; CAP27047.1; -; Genomic_DNA.
DR   RefSeq; XP_002642404.1; XM_002642358.1.
DR   AlphaFoldDB; Q61R02; -.
DR   SMR; Q61R02; -.
DR   STRING; 6238.CBG06798; -.
DR   EnsemblMetazoa; CBG06798.1; CBG06798.1; WBGene00029014.
DR   GeneID; 8584398; -.
DR   KEGG; cbr:CBG_06798; -.
DR   CTD; 8584398; -.
DR   WormBase; CBG06798; CBP01738; WBGene00029014; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   HOGENOM; CLU_003041_26_4_1; -.
DR   InParanoid; Q61R02; -.
DR   OMA; IQFEDHM; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; IEA:UniProt.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..577
FT                   /note="Probable ATP-dependent RNA helicase DDX55 homolog"
FT                   /id="PRO_0000252216"
FT   DOMAIN          40..218
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          231..393
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          508..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           7..37
FT                   /note="Q motif"
FT   MOTIF           166..169
FT                   /note="DEAD box"
FT   COMPBIAS        533..562
FT                   /note="Basic and acidic 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   577 AA;  65738 MW;  E9031404175DC309 CRC64;
     MTSKVGAVAT KTYREKLGPE ILEVFDKSYK SFTDVQVLAG THLLNLSDVV VESPTGSGKT
     LAFVLPMMRM IQNARLQPNE IGALILSPSR ELCSQIVNVI KPFAEKMKLN VETVTGGQKV
     DKNIKMFKNK DINILVATPG RLFQIIQHEK TMIARAMKGV QLLVIDEADR FNEIQFEDHM
     REILSCIPKQ RRTGLFSATQ VKEEDDLMVF GLRNAKQVKV SQERNSAAPS TLKNYFVECP
     ADEKTSVCLE FIRQRTDKKV LIFFPSCNSV RYFHKIFERC LTKRPLFAVH GKCSNPHRAA
     QIKAFSESTN GVMISTDVMA RGIDITDIDW VIQYDLPKHS SWFVHRAGRT ARCGRDGNAL
     ILIATEQLAY VSFLDNHEKV KLEEVKVPTS TSRKAEELRQ KMIKIQVSDR AILELGTRAF
     VSHIESYAKH DCHLICSLDD LNVVGLANSY ALLRLPKMRE LAQRKDLNQF DRSDIETSEI
     KYADPKLEAN RDTVMKEKHE KKIETLAAKE KKRREKEARK MKRAGGRFKS RATGANAEEK
     RAKKRKSEEE DDAQNDIRLL KKIKRGKLSK KEIKDVL