ID   DBP10_NEOFI             Reviewed;         934 AA.
AC   A1DNG2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=ATP-dependent RNA helicase dbp10;
DE            EC=3.6.4.13;
GN   Name=dbp10; ORFNames=NFIA_056820;
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 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. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS027698; EAW16333.1; -; Genomic_DNA.
DR   RefSeq; XP_001258230.1; XM_001258229.1.
DR   AlphaFoldDB; A1DNG2; -.
DR   SMR; A1DNG2; -.
DR   STRING; 36630.CADNFIAP00004384; -.
DR   EnsemblFungi; EAW16333; EAW16333; NFIA_056820.
DR   GeneID; 4584745; -.
DR   KEGG; nfi:NFIA_056820; -.
DR   VEuPathDB; FungiDB:NFIA_056820; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
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; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10.
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   PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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..934
FT                   /note="ATP-dependent RNA helicase dbp10"
FT                   /id="PRO_0000281716"
FT   DOMAIN          121..293
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          361..515
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           90..118
FT                   /note="Q motif"
FT   MOTIF           241..244
FT                   /note="DEAD box"
FT   COMPBIAS        339..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..891
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..934
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   934 AA;  103372 MW;  1241FDC5CF4FDF9C CRC64;
     MPHRAASPAM SENEFDITGA LFQNDSDSDN EQPSAKSKRQ PPKKVPSQAL DFLGDVNEDD
     DDDEAFIAEQ QTSANRKASN LKGRTVKKGG GFQAMGLSAN LLKAIARKGF SVPTPIQRKT
     IPVIMDDQDV VGMARTGSGK TAAFVIPMIE KLKSHSTKVG ARGLILSPSR ELALQTLKVV
     KELGRGTDLK SVLLVGGDSL EEQFAMMAGN PDIVIATPGR FLHLKVEMNL DLSSIRYVVF
     DEADRLFEMG FAAQLTEILH GLPANRQTLL FSATLPKSLV EFARAGLQEP TLVRLDTESK
     ISPDLQNAFF SVKSSEKEGA LLYILQEVIK MPTGPTEVSQ QRKEEDASAK NWKNKKRKRA
     EMEKAVNMRE SPTKHSTIVF AATKHHVDYL YSLLSEAGFA VSYVYGSLDQ TARKIQVQNF
     RTGMTNILVV TDVAARGIDI PILANVINYD FPSQPKIFIH RVGRTARAGR KGWSYSLVRD
     ADAPYLLDLQ LFLGRRLVVG REFGDQVNFA EDVVTGSLPR DGLSQSCEWV TKVLDDNADL
     AAQRTVAAKG EKLYMRTRNS ASLESAKRSK QVVSSDNWTS IHPLFQDETS NLEAEREKML
     ARIGGYRPPE TIFEVNNRRM GKHENVDALD TIKRVRTTLE SKKKRAQANE KSEFLEDASD
     DEKAANEAGE NENEGAFSDE DDDVPTGVAD NMSMASDSEL EVTFSSYSQS KENKAKKASA
     ASFQNPEYFM SYTPNNNSLV EDRAYGVHSG TNSNFAQASR SATMDLAGDD GGRGFGEART
     LMRWDKRHKK YVARQNDEDG SKGTRLVRGE SGAKIAASFR SGRFDAWKRG NRLGRLPRVG
     EAEAPNLTAG LNAAISGKRF RHRKEQAPKR ADPLRGDYEK MKKKAELAKE RAMSKAGGAA
     PRGKSELKNT DDIRIARKLK QKRREKNARP SRKK