ID   DBP8_ASPTN              Reviewed;         527 AA.
AC   Q0CNX1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=ATP-dependent RNA helicase dbp8;
DE            EC=3.6.4.13;
GN   Name=dbp8; ORFNames=ATEG_04613;
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 40S ribosomal subunit
CC       biogenesis and is required for the normal formation of 18S rRNAs
CC       through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC       vegetative growth (By similarity). {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. DDX49/DBP8
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476599; EAU35060.1; -; Genomic_DNA.
DR   RefSeq; XP_001213791.1; XM_001213791.1.
DR   AlphaFoldDB; Q0CNX1; -.
DR   SMR; Q0CNX1; -.
DR   STRING; 341663.Q0CNX1; -.
DR   EnsemblFungi; EAU35060; EAU35060; ATEG_04613.
DR   GeneID; 4320029; -.
DR   VEuPathDB; FungiDB:ATEG_04613; -.
DR   eggNOG; KOG0340; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   OMA; EIKQESM; -.
DR   OrthoDB; 744428at2759; -.
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: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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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..527
FT                   /note="ATP-dependent RNA helicase dbp8"
FT                   /id="PRO_0000281711"
FT   DOMAIN          117..296
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          324..486
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           86..114
FT                   /note="Q motif"
FT   MOTIF           239..242
FT                   /note="DEAD box"
FT   COMPBIAS        1..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   527 AA;  57521 MW;  9E03E22ED26E1E4D CRC64;
     MENDHSSSDE HEHENPELQT RAPKRRRLSE TSEDDEYVAA PTPLPTLSRI KKKEPKDENK
     DTSTGTDNPV LIKDALEMGL QDAGESSFKA LNVAPWLIGS LTTMAVRKPT AIQRACIPEI
     LKGRDCIGGS RTGSGKTIAF AVPILQKWAE DPFGIFAVVL TPTRELALQI YEQFKAISAP
     QSMKPVLITG GTDMRPQALA LSQRPHVVIA TPGRLADHIQ TSGEDTVRGL KRVRMVVLDE
     ADRLLAPGPG SMLPDVETCL SALPPSSERQ TLLFTATVTP EVRALKSMPR ASTKPPVFVT
     EIEAGGTTSA GADGAAPKST LPPTLKQTYL KVPMTHREAF LHVLLSTDGN AGKPAIIFCN
     HTKTADLLER LLRRLAHRVT SLHSLLPQSE RSSNLARFRA SAARILVATD VASRGLDIPS
     VALVVNYDVP RNPDDYVHRV GRTARAGRRG EAVTLVGQRD VQLVLAIEER VGRQMEEWSE
     EGVSVEGRVV RTGVLKEVGS AKREALIEIE EGRDVLGRKR NKLKKVR