ID   DBP9_VANPO              Reviewed;         597 AA.
AC   A7TPC9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; ORFNames=Kpol_1009p3;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDO15857.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DS480441; EDO15857.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001643715.1; XM_001643665.1.
DR   AlphaFoldDB; A7TPC9; -.
DR   SMR; A7TPC9; -.
DR   STRING; 436907.A7TPC9; -.
DR   EnsemblFungi; EDO15857; EDO15857; Kpol_1009p3.
DR   GeneID; 5543990; -.
DR   KEGG; vpo:Kpol_1009p3; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; A7TPC9; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000267; 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   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..597
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000310257"
FT   DOMAIN          49..235
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          248..477
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          340..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           17..45
FT                   /note="Q motif"
FT   MOTIF           181..184
FT                   /note="DEAD box"
FT   COMPBIAS        340..355
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..583
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   597 AA;  68175 MW;  0ECCDFB9B4AD28E6 CRC64;
     MSSSEVLAPE AYIDDSISFE SLQLDTRLLQ AIKRNGFKNP TLIQSHAIPL ALQEKRDIIA
     KAATGCGKTL AYLIPVIQTI LDYKKTNTDK IDGTSNTLGI ILVPTRELAQ QVNDVLDKMI
     LYCSNDIRSL NISSDMPSSV LTSLLLEKPE IIIATPGKLM TLLDTNVESV SLEELKFLVI
     DEVDLVLTFG YKEDLSKIAE YLPLKKNLQT FLMSATLNDD IQELKKEFCR APAILKFNDD
     EISKDKNKLI QYYVKTSEFD KFLLCYVIFK LGLIKGKTLI FVNNIDRGYR LKLVLEQFGI
     KSCILNSELP ANSRQHIVDQ FNKNVYHLLI ATDDTEYIKE EDEENDDEIE TNSEEQDKVE
     DSNDTKDKKG KKASKIKKDK EFGVSRGVDF QNVACVLNFD LPTTAKSYVH RIGRTARAGK
     TGTAISFVVP LKEFGKHKPS MYQSTKRDEK ILSRIIKQQS KLGLELQPYS FDTKQIEGFR
     YRMEDGFRAV TQVAIREARV KELKDELLAS EKLKRHFEEN PQELQSLRHD KELHPSRVQQ
     HLKRVPDYLL PAEAREGKKK VGFVPFHSVK KSNRHKKNNK VFKKRSGSKS DPLKNFK