ID   DBP3_NEOFI              Reviewed;         503 AA.
AC   A1DG51;
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 dbp3;
DE            EC=3.6.4.13;
GN   Name=dbp3; ORFNames=NFIA_083090;
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-dependent RNA helicase required for 60S ribosomal subunit
CC       synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC       site A3, which is necessary for the normal formation of 25S and 5.8S
CC       rRNAs (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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS027696; EAW18358.1; -; Genomic_DNA.
DR   RefSeq; XP_001260255.1; XM_001260254.1.
DR   AlphaFoldDB; A1DG51; -.
DR   SMR; A1DG51; -.
DR   STRING; 36630.CADNFIAP00007592; -.
DR   EnsemblFungi; EAW18358; EAW18358; NFIA_083090.
DR   GeneID; 4586812; -.
DR   KEGG; nfi:NFIA_083090; -.
DR   VEuPathDB; FungiDB:NFIA_083090; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_1_5_1; -.
DR   OMA; KKKTHDM; -.
DR   OrthoDB; 471730at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S 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; IPR000629; RNA-helicase_DEAD-box_CS.
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.
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..503
FT                   /note="ATP-dependent RNA helicase dbp3"
FT                   /id="PRO_0000281698"
FT   DOMAIN          116..292
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          307..472
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           104..112
FT                   /note="Q motif"
FT   MOTIF           239..242
FT                   /note="DEAD box"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   503 AA;  54970 MW;  4C3E07FBF4ABC427 CRC64;
     MAKRVQHEGG DYRPQKRSKN ERNGEGSKVS PSAEAIRNEL DPISDATYVQ SPALGDLSQI
     EIDQFLAKHC IKVTDSSEAP PLRPIISFSH LPSSFSKIYD PLSSFSSPTP IQSATWPLLF
     AGRDVIGIAE TGSGKTLAFG LPCIKKILDS GKVKRKHARP AAVIISPTRE LAMQIYDQLS
     KFGASVDIRV TCIYGGVKKD EQREALKTAA IVVATPGRLK DLQNDGSVDL GKVKYLVLDE
     ADRMLDKGFE QDIKDIIRSM PDSKRQTVMF TATWPPSVRD LAATFMTSAV TVTIGGDPSA
     DPRANTRIKQ VVEVVKPQEK EARLVQLLNR SQRGAAVCDK VLVFCLYKKE AVRVERLLRT
     KNFKVAGIHG DLNQHERFKS LEAFKTGAAT VLVATDVAAR GLDIPSVKLV INVTFPLTVE
     DYVHRIGRTG RAGADGHAIT LFTETDKAQS GALINVLRAA KQDVPDALLK FGTTVKKKQH
     GAYGAFFKDV DTSKSATKIV FDE