ID   DBP4_KLULA              Reviewed;         770 AA.
AC   Q6CRF4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; OrderedLocusNames=KLLA0D09504g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2 (By similarity).
CC       {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 the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes (By similarity). {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. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR382124; CAH00581.1; -; Genomic_DNA.
DR   RefSeq; XP_453485.1; XM_453485.1.
DR   AlphaFoldDB; Q6CRF4; -.
DR   SMR; Q6CRF4; -.
DR   STRING; 28985.XP_453485.1; -.
DR   EnsemblFungi; CAH00581; CAH00581; KLLA0_D09504g.
DR   GeneID; 2892880; -.
DR   KEGG; kla:KLLA0_D09504g; -.
DR   eggNOG; KOG0343; Eukaryota.
DR   HOGENOM; CLU_003041_26_1_1; -.
DR   InParanoid; Q6CRF4; -.
DR   OMA; YDKMFER; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
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; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
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..770
FT                   /note="ATP-dependent RNA helicase DBP4"
FT                   /id="PRO_0000232201"
FT   DOMAIN          72..246
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          276..435
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          596..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           41..69
FT                   /note="Q motif"
FT   MOTIF           194..197
FT                   /note="DEAD box"
FT   COMPBIAS        650..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   770 AA;  87827 MW;  E0022DA405E12264 CRC64;
     MAKKQKHNTQ QRKLIRERDS QKIKDLETKV EEYNPKIAKA NLFQDLPISE QTLKGLKEAA
     FIKLTEIQRE SIPLSLKGHD VLGAAKTGSG KTLAFLIPVI EKLYREKWTD MDGLGALIIS
     PTRELAMQIY EVLSKIGKHT TFSAGLVIGG KDVTFEKERI SRINILIGTP GRILQHMDQA
     VGFNTSNLQL LVLDEADRCL DMGFKRTLDA IINNLPASRQ TLLFSATQSQ SLDDLARLSL
     TDYKQVGTME VLNANSSSAT PESLQQSYIE VPLPDKLDIL FSFIKSHLKS KLIVFLSSSK
     QVHFVYETFR KLQPGISLMH LHGRQKQTAR TETLDKFSRA QHVCLFSTDV VARGIDFPSV
     DWVIQVDCPE DVDTYIHRVG RAARFGKEGK SLIMLTPEEE EGFLKRLKTK NIEPSRLNIK
     QSKKKSIKPQ LQSLLFKDPE LKYLGQKAFI SYVRSIYIQK DKEVFHFDKI PLEQFANSLG
     LPGAPKIKMR GMKSIEKAKE LKNTSRQLLT LAKANDEGDV IKENKPEVRT RYDKMFERKN
     QTVLSEHYLN VTKAQAHDDE DEDFIMVKRQ DHELNEAELP ELLVPTSKRA QKKALSRKAT
     LASNGNPTKV KFDDDGKAHP VYELEDEQDF RQNGNSEKQK EEFLSKEAEL MAKVDVEDKQ
     VAKEKRQEKK RKRLEAMRKE MEADMEDSDY EDEPVAYLGT GNLSDDMQSG ADTEDDSQDE
     RQPRKKSKYA DSSEDEEEEE RTTERDRIIE VEEPQTLEDL ESLTANLIGS