ID   DDX55_BOVIN             Reviewed;         601 AA.
AC   Q2NL08;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC111255; AAI11256.1; -; mRNA.
DR   RefSeq; NP_001039472.1; NM_001046007.2.
DR   AlphaFoldDB; Q2NL08; -.
DR   SMR; Q2NL08; -.
DR   STRING; 9913.ENSBTAP00000009556; -.
DR   PaxDb; Q2NL08; -.
DR   PRIDE; Q2NL08; -.
DR   GeneID; 508581; -.
DR   KEGG; bta:508581; -.
DR   CTD; 57696; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   eggNOG; KOG0345; Eukaryota.
DR   InParanoid; Q2NL08; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000009136; 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; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..601
FT                   /note="ATP-dependent RNA helicase DDX55"
FT                   /id="PRO_0000252209"
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          502..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT   MOTIF           171..174
FT                   /note="DEAD box"
FT   COMPBIAS        502..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..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"
FT   MOD_RES         545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHQ9"
FT   MOD_RES         595
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHQ9"
SQ   SEQUENCE   601 AA;  68601 MW;  6FAB7FA203BF4008 CRC64;
     MEHVTEGSWE SLPVPLHPKV LSVLRELGFP YMTPVQSATI PLFMKNKDVA AEAVTGSGKT
     LAFVIPIEEI LLRREEKFKK SQVGAIIITP TRELAVQIEE VLSHFTKPFP QFSQILWIGG
     RNPGEDVARF KELGGNIIVA TPGRLEDMFR RKAEGLDLAS CVRSLEVLVL DEADRLLDMG
     FETSINTILE FLPKQRRTGL FSATQTQEVE NLVRAGLRNP VRISVKEKGV AASSTQKTPS
     RLENHYMVCK ADEKFNQLVH FLRNHKQEKH LVFFSTCACV EYYGKALETL VKGVKIMCIH
     GKMKYKRNKI FMEFRKLQSG ILVCTDVMAR GIDIPEVNWV LQYDPPSNAS AFVHRCGRTA
     RIGHGGSALV FLLPMEESYI SFLAINQKCP LQEMKLQKNT ADLLPKLKAM ALGDRAVFEK
     GMKAFVSYVQ AYAKHECNLI FRLKDLDFAS LARGFALLRM PKMPELRGKQ FPDFVPVDVN
     TDTIPFKDKI REKQRQKQLL EQQRKEKTEN DGRRKFIKNK AWSKQKAKKE KKKKLTEKRK
     REEGSDVEDE DMEELLNDTR LLKKFKKGKI TEEEFEKGLL TSGKRSTNKA DLEISDLEDD
     C