ID   DBP9_ASPTN              Reviewed;         619 AA.
AC   Q0CY48;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=ATP-dependent RNA helicase dbp9;
DE            EC=3.6.4.13;
GN   Name=dbp9; ORFNames=ATEG_01386;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU38143.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476595; EAU38143.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001208751.1; XM_001208751.1.
DR   AlphaFoldDB; Q0CY48; -.
DR   SMR; Q0CY48; -.
DR   STRING; 341663.Q0CY48; -.
DR   GeneID; 4315699; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000007963; 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:0003678; F:DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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..619
FT                   /note="ATP-dependent RNA helicase dbp9"
FT                   /id="PRO_0000281719"
FT   DOMAIN          58..236
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          247..484
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           27..55
FT                   /note="Q motif"
FT   MOTIF           184..187
FT                   /note="DEAD box"
FT   COMPBIAS        362..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   619 AA;  69057 MW;  27422BDAC21BBB15 CRC64;
     MKRKLDANDV PSPEAADDSV KNDVDNLDFE SLNLDPRLRQ ALVKEKFTKP TLVQAKAIPL
     ALEGKDILAR AKTGSGKTAA YVLPILQTIL QKKANDPSLK ATTGLILVPT RELAEQVQNV
     ITTFAAFCGK DVRSVNLTQK VSDAVQRTML ADYPDLIVST PSRVIANLGS SALSLENLTH
     LVIDEADLVL SYGYDEDINA LAKAIPRGVQ TFLMSATLTA EVDTLKGLFC RSPVILKLED
     KDDQGSGVSQ FVVKCAEDEK FLLTYVIFKL QLIKGKVIIF VGDVDRCYRV KLFLEQFGIK
     SCVLNSELPV NSRLHVVQEF NKGVYDIIIA ADEQEVMGAR KSKKSKEAEE NDAGEAAGSS
     DEDEGEAQKP STTRSDKPSE KRRKTAGKDK DYGISRGIDF QNVACVLNFD LPTTSKSYTH
     RIGRTGRAGK TGMALSFVVP ADQFGKHKPT SFPTAKHDET VLAKITKRQA KLGHEVKPYH
     FEMKQVDAFR YRMTDALRSI TRLAVQEARA REIRQELIKS EKLKRHFEEN PEELRQLRHD
     DELRSARIQP HLKHIPDYLM PSKGKKGISS ENVGYVGFRK TSENRIRKAR EKNRGKGKGR
     NYAGVKKVDP LKTFNRGRK