DDX59_RAT
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 03-AUG-2022, entry version 123.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 project:
RT 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 RUVBL1/RUVBL2
CC complex in the presence of ADP. {ECO:0000250|UniProtKB:Q5T1V6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T1V6}. Nucleus
CC {ECO:0000250|UniProtKB:Q5T1V6}. Note=Exhibits granular localization in
CC 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 box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX59 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC081871; AAH81871.1; -; mRNA.
DR RefSeq; NP_001005535.1; NM_001005535.2.
DR RefSeq; NP_001177749.1; NM_001190820.1.
DR AlphaFoldDB; Q66HG7; -.
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 GeneTree; ENSGT00940000158639; -.
DR InParanoid; Q66HG7; -.
DR OrthoDB; 400908at2759; -.
DR PRO; PR:Q66HG7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000042451; Expressed in ovary and 19 other tissues.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 3.
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; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..589
FT /note="Probable ATP-dependent RNA helicase DDX59"
FT /id="PRO_0000282715"
FT DOMAIN 234..375
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 399..549
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 104..133
FT /note="HIT-type"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 203..231
FT /note="Q motif"
FT MOTIF 323..326
FT /note="DEAD box"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1V6"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1V6"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1V6"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="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
