GenomeNet

Database: UniProt
Entry: Q2NL08
LinkDB: Q2NL08
Original site: Q2NL08 
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   16-OCT-2019, entry version 76.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
DR   EMBL; BC111255; AAI11256.1; -; mRNA.
DR   RefSeq; NP_001039472.1; NM_001046007.2.
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; KOG0345; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   HOGENOM; HOG000268803; -.
DR   InParanoid; Q2NL08; -.
DR   KO; K14809; -.
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:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN         1    601       ATP-dependent RNA helicase DDX55.
FT                                /FTId=PRO_0000252209.
FT   DOMAIN       40    223       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      254    402       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         9     37       Q motif.
FT   MOTIF       171    174       DEAD box.
FT   COMPBIAS    487    569       Lys-rich.
FT   MOD_RES     545    545       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8NHQ9}.
FT   MOD_RES     595    595       Phosphoserine.
FT                                {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
//
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