ID   DBP9_LODEL              Reviewed;         606 AA.
AC   A5E572;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; ORFNames=LELG_04761;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
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DR   EMBL; CH981530; EDK46580.1; -; Genomic_DNA.
DR   RefSeq; XP_001523948.1; XM_001523898.1.
DR   AlphaFoldDB; A5E572; -.
DR   SMR; A5E572; -.
DR   STRING; 379508.A5E572; -.
DR   EnsemblFungi; EDK46580; EDK46580; LELG_04761.
DR   GeneID; 5231059; -.
DR   KEGG; lel:LELG_04761; -.
DR   VEuPathDB; FungiDB:LELG_04761; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; A5E572; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000001996; 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..606
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000294670"
FT   DOMAIN          52..232
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          261..488
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          336..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           20..48
FT                   /note="Q motif"
FT   MOTIF           178..181
FT                   /note="DEAD box"
FT   COMPBIAS        370..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   606 AA;  69234 MW;  F53609137E4CA415 CRC64;
     MSLKSTKTTA ASETYLDDET TWDSLNLDPR LLQAIDKLGF ENPTLIQSSA IPLALEEKRD
     IIAKASTGSG KTAAYAIPII QNIMVQGSQL GTQSVVLVPT RELSNQVYQF MEQLIKFSNN
     KIGILNLSSN YSDQVLKSLL INKPEIIIST PSKLIQTLEA HEGKDIIDLS TVKNLTIDEV
     DLILSFGYKD DLQKLESYLP VKKNLQTFLM SATVNDDLNE LKAKFCTKPA ILKLDDDQSN
     NNKLVQFYAK TTEFDKFLLS YVIFKLNLIK GKTIVFVNNI DRGYRLKLFL EQFGIRCCIL
     NSELPINSRL HIVEEFNKNV YHLLIATDDI SVEKEEVDEV DEGEEEHEDA ADADEKKQQN
     NNNNNNNHNN NNKEHKEVLK KNEKNKKHSS KKDKEYGVSR GVDFRNVACV LNFDLPTTSK
     SYVHRVGRTA RAGKSGMALS FVIPEKEVGK HKTASLRSAK KDEKVLNRIV KQQQKNGFEI
     KPYQFDMKQV EGFRYRADDA FRAVTQTAIR EARVKELKNE LINSEKLKRF FQENPRDLAS
     LRHDKELHPA RVQAHLKRTP QYLLPESARL DVKNLGFIPF HKNKVGKYRK KSKGTKKRDP
     LKSFKK