ID   DBP9_YEAS7              Reviewed;         594 AA.
AC   A7A1G0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 9;
GN   Name=DBP9; ORFNames=SCY_3838;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits and is required for the normal formation of 25S and
CC       5.8S rRNAs. {ECO:0000250}.
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 with DBP6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFW02000170; EDN59364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7A1G0; -.
DR   SMR; A7A1G0; -.
DR   EnsemblFungi; EDN59364; EDN59364; SCY_3838.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..594
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000310258"
FT   DOMAIN          49..233
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          246..476
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          339..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           17..45
FT                   /note="Q motif"
FT   MOTIF           179..182
FT                   /note="DEAD box"
FT   COMPBIAS        348..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..581
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   594 AA;  68060 MW;  CCE8E0AF8B4071D7 CRC64;
     MSYEKKSVEG AYIDDSTTFE AFHLDSRLLQ AIKNIGFQYP TLIQSHAIPL ALQQKRDIIA
     KAATGSGKTL AYLIPVIETI LEYKKTIDNG EENGTLGIIL VPTRELAQQV YNVLEKLVLY
     CSKDIRTLNI SSDMSDSVLS TLLMDQPEII VGTPGKLLDL LQTKINSISL NELKFLVVDE
     VDLVLTFGYQ DDLNKIGEYL PLKKNLQTFL MSATLNDDIQ ALKQKFCRSP AILKFNDEEI
     NKNQNKLLQY YVKVSEFDKF LLCYVIFKLN LIKGKTLIFV NNIDRGYRLK LVMEQFGIKS
     CILNSELPVN SRQHIVDQFN KNVYQLLIAT DDTEYIKEED DEIEEGHNTE NQEEKSLEGE
     PENDKKPSKK KKVQVKKDKE YGVSRGVDFK NVACVLNFDL PTTAKSYVHR VGRTARGGKT
     GTAISFVVPL KEFGKHKPSM LQTAKKDERI LSRIIKQQSK LGLELQPYKF DQKQVEAFRY
     RMEDGFRAVT QVAIREARVK ELKQELLASE KLKRHFEENP KELQSLRHDK ELHPARVQQH
     LKRVPDYLLP ESARGNGTKV KFVPFHNAKK RHSHKKGRVS KPKNGKVDPL KNFK