ID   DBP4_YARLI              Reviewed;         740 AA.
AC   Q6CGD1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; OrderedLocusNames=YALI0A20328g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382127; CAG84219.1; -; Genomic_DNA.
DR   RefSeq; XP_500281.1; XM_500281.1.
DR   AlphaFoldDB; Q6CGD1; -.
DR   SMR; Q6CGD1; -.
DR   STRING; 4952.CAG84219; -.
DR   PRIDE; Q6CGD1; -.
DR   EnsemblFungi; CAG84219; CAG84219; YALI0_A20328g.
DR   GeneID; 2906391; -.
DR   KEGG; yli:YALI0A20328g; -.
DR   VEuPathDB; FungiDB:YALI0_A20328g; -.
DR   HOGENOM; CLU_003041_26_1_1; -.
DR   InParanoid; Q6CGD1; -.
DR   OMA; YDKMFER; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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..740
FT                   /note="ATP-dependent RNA helicase DBP4"
FT                   /id="PRO_0000232204"
FT   DOMAIN          70..244
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          257..421
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           39..67
FT                   /note="Q motif"
FT   MOTIF           192..195
FT                   /note="DEAD box"
FT   COMPBIAS        7..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..727
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   740 AA;  83760 MW;  4095B16132F1D4BF CRC64;
     MKKRADPRKI KREEHKQKLS KLQERVDNFG EDEADKEVSK FEELPLSEAT IEGLKNSHYV
     TCTDVQKRAI PPALQGHDLL GAARTGSGKT LAFLVPVLEC LFRNKWSDVD GLGALVISPT
     RELAVQIFQV LRKIGRCHSF SAGLVIGGKD VAMEADRLAK LNILICTPGR LLQHMDQTSG
     FDLSNVKMLV LDEADRILDM GFKKTMDAIL ENLPVDRQTL LFSATQTKSV SDLARLSLAD
     PKYISANPDT TSSTPKNLEQ NYVCVELQDK LDTLWGFLRT HTKFKIIVFF SSSKQVRYVY
     ETFRTLQPGI PLLHLHGKQK QGARMDVVSK FSKASSSCLF ATDIVARGID FPAVHWVVQV
     DCPEDAATYI HRVGRSARFG KSGKALLFLT PTEEPAMIQR LEAKHIPINK LTIRPNKKKS
     IKNQLQALCF KSPEIKYLGQ KAFISYYKSI FIQKDKEIFQ FEKIPSEAFA ESLGLPGAPQ
     IKLGKSAEKM KEEANAKKNQ SRALQKLMRA GDDGVVSDDE KEVRTKMDRM FERKNQNVLS
     DHYLNMVKGD ADEDEETGDF MTVKRQDHNL ESDDDEDIAN LPTSKRAAKQ ALSKKQSLKN
     KGLGTKTLFD DEGAPHALYE FDDEEDFKAA GPVESQVKEF VDRETKDMEE ADVGDKELVK
     QKRAEKKRKR KEIERLRELD EYDEESEEEG DSEEEQAAKK PKWFQRDESS DEEEDDGVLE
     VEEPTTLEDL ESLTSKLLKK