GenomeNet

Database: UniProt
Entry: Q66HG7
LinkDB: Q66HG7
Original site: Q66HG7 
ID   DDX59_RAT               Reviewed;         589 AA.
AC   Q66HG7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-OCT-2019, entry version 114.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX59;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 59;
DE   AltName: Full=Zinc finger HIT domain-containing protein 5 {ECO:0000250|UniProtKB:Q5T1V6};
GN   Name=Ddx59; Synonyms=Znhit5 {ECO:0000250|UniProtKB:Q5T1V6};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- SUBUNIT: Interacts (via HIT-type zinc finger) with the
CC       RUVBL1/RUVBL2 complex in the presence of ADP.
CC       {ECO:0000250|UniProtKB:Q5T1V6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T1V6}.
CC       Nucleus {ECO:0000250|UniProtKB:Q5T1V6}. Note=Exhibits granular
CC       localization in the nucleus, as well as in the cytoplasm.
CC       {ECO:0000250|UniProtKB:Q5T1V6}.
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. DDX59
CC       subfamily. {ECO:0000305}.
DR   EMBL; BC081871; AAH81871.1; -; mRNA.
DR   RefSeq; NP_001005535.1; NM_001005535.2.
DR   RefSeq; NP_001177749.1; NM_001190820.1.
DR   SMR; Q66HG7; -.
DR   STRING; 10116.ENSRNOP00000047251; -.
DR   PhosphoSitePlus; Q66HG7; -.
DR   PaxDb; Q66HG7; -.
DR   PRIDE; Q66HG7; -.
DR   Ensembl; ENSRNOT00000043798; ENSRNOP00000049858; ENSRNOG00000042451.
DR   GeneID; 289402; -.
DR   KEGG; rno:289402; -.
DR   UCSC; RGD:1359520; rat.
DR   CTD; 83479; -.
DR   RGD; 1359520; Ddx59.
DR   eggNOG; KOG0331; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000158639; -.
DR   HOGENOM; HOG000006599; -.
DR   InParanoid; Q66HG7; -.
DR   KO; K19466; -.
DR   OrthoDB; 400908at2759; -.
DR   PRO; PR:Q66HG7; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000042451; Expressed in 9 organ(s), highest expression level in skeletal muscle tissue.
DR   ExpressionAtlas; Q66HG7; baseline and differential.
DR   Genevisible; Q66HG7; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR007529; Znf_HIT.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04438; zf-HIT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; Cytoplasm; Helicase; Hydrolase;
KW   Isopeptide bond; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    589       Probable ATP-dependent RNA helicase
FT                                DDX59.
FT                                /FTId=PRO_0000282715.
FT   DOMAIN      234    375       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      399    549       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   ZN_FING     104    133       HIT-type.
FT   NP_BIND     247    254       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       203    231       Q motif.
FT   MOTIF       323    326       DEAD box.
FT   MOD_RES      64     64       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5T1V6}.
FT   MOD_RES     156    156       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5T1V6}.
FT   MOD_RES     160    160       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5T1V6}.
FT   CROSSLNK     26     26       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q5T1V6}.
SQ   SEQUENCE   589 AA;  65066 MW;  52C0CD853C592D1E CRC64;
     MFVPRSLKLK RNSNDDLKSC EAKKSKPEAA GLQLEGNRET LVLESVTKEA VTADRPGSAS
     STSSPSCQLA EVCSTGPDQG VKDSHPSEEP VKSFSKTQRW PEPGEPVCVV CGRYGEYICD
     KTDEDVCSLE CKAKHLLQVK EEEGSLKPSS PQGAASEPES PLDAFYVYKE HPFIVALRDD
     QIETLKQQLG ISVQGQEVAR PIIDFEHCGF PETLNQNLKK SGYEVPTPIQ MQMIPVGLLG
     RDILASADTG SGKTAAFLLP VIIRALPEDK TPSALILTPT RELAIQIERQ AKELMRGLPR
     MKTVLLVGGL PLPPQLYRLQ QHVKADTMLK MGFQQQVLDV LEHTPSDCQT VLVSATIPDS
     IDQLADQLLH NPVRIVTGDK NLPCSSVRQI ILWVEDPAKK KKLFEILNDQ KLFKPPVLVF
     VDCKLGADLL SEAVQKITGL SSTSIHSEKS QVERREILKG LLEGDYEVVV STGILGRGLD
     LVNVKLVVNF DMPSSLDEYV HQVGRVGRLG QNGTAITFIN NNSKRLFWDV AKRVKPTGSI
     LPPQLLNSPY LHEQKRKEQQ KDRQTQSSLV TGANLMDIIR KHEKSSSQK
//
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