ID   DBP8_NEOFI              Reviewed;         526 AA.
AC   A1D6X9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent RNA helicase dbp8;
DE            EC=3.6.4.13;
GN   Name=dbp8; ORFNames=NFIA_066370;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027690; EAW21473.1; -; Genomic_DNA.
DR   RefSeq; XP_001263370.1; XM_001263369.1.
DR   AlphaFoldDB; A1D6X9; -.
DR   SMR; A1D6X9; -.
DR   STRING; 36630.CADNFIAP00006110; -.
DR   EnsemblFungi; EAW21473; EAW21473; NFIA_066370.
DR   GeneID; 4589684; -.
DR   KEGG; nfi:NFIA_066370; -.
DR   VEuPathDB; FungiDB:NFIA_066370; -.
DR   eggNOG; KOG0340; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   OMA; EIKQESM; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000006702; 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..526
FT                   /note="ATP-dependent RNA helicase dbp8"
FT                   /id="PRO_0000281712"
FT   DOMAIN          127..306
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          338..485
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           96..124
FT                   /note="Q motif"
FT   MOTIF           249..252
FT                   /note="DEAD box"
FT   COMPBIAS        28..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   526 AA;  57115 MW;  CCD71C3474049941 CRC64;
     MASPVPSEPV SEDTHDSSSG SEVEQSEIST RAPKRRRLSE SSDDSDDSYV APAPLPTLSR
     IKKKGAPDAK PAAPAGQDNP VLIRDALEIG LREEASSFAA LNVAPWLVGS LTTMAVRKPT
     AIQKACIPEI LKGRDCIGGS RTGSGKTIAF SVPMLQKWAE DPFGIFGVVL TPTRELALQI
     FEQIKAISAP QSMKPVLITG GTDMRPQAIA LAGRPHVVIA TPGRLADHIK SSGEDTVCGL
     KRVRMVVLDE ADRLLASGPG SMLPDVETCL SALPPSSERQ TLLFTATVTP EVRALKNMPR
     SANKPPVFVT EISTENQGSI PPTLKQTYLK VPLTHREAFL HVLLSTEDNA SRPAIIFCNH
     TKTADLLERM LRRLTHRVTS LHSLLPQSER NANLARFRAS AARILVATDV ASRGLDIPTV
     SLVINYDVPR NPDDYVHRVG RTARAGRSGE AITLVGQRDV QLVLAIEERV GRQMEEWSEE
     GVSIEGRLVR TGVLKEVGEA KREAMGEIDE GRDVLGRKRN KLKKVR