ID   DBP10_ASPCL             Reviewed;         935 AA.
AC   A1CTZ6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP-dependent RNA helicase dbp10;
DE            EC=3.6.4.13;
GN   Name=dbp10; ORFNames=ACLA_084780;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06783.1; -; Genomic_DNA.
DR   RefSeq; XP_001268209.1; XM_001268208.1.
DR   AlphaFoldDB; A1CTZ6; -.
DR   SMR; A1CTZ6; -.
DR   STRING; 5057.CADACLAP00007338; -.
DR   PRIDE; A1CTZ6; -.
DR   EnsemblFungi; EAW06783; EAW06783; ACLA_084780.
DR   GeneID; 4700481; -.
DR   KEGG; act:ACLA_084780; -.
DR   VEuPathDB; FungiDB:ACLA_084780; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000006701; 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..935
FT                   /note="ATP-dependent RNA helicase dbp10"
FT                   /id="PRO_0000281713"
FT   DOMAIN          120..292
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          360..514
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           89..117
FT                   /note="Q motif"
FT   MOTIF           240..243
FT                   /note="DEAD box"
FT   COMPBIAS        29..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..894
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..935
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   935 AA;  103007 MW;  B17650287889C359 CRC64;
     MAPRAASPAL SENEFDITGA LFQNDSESDN ERSSAKSKRQ PKKKIPSQDL DFLGDVNDDD
     GDEAFIAQQQ TSANRKASNL KGRTVKKGGG FQAMGLSANL LKAIARKGFS VPTPIQRKTI
     PVIMDDQDVV GMARTGSGKT AAFVIPMIEK LRSHSTKVGA RGLILSPSRE LALQTLKVVK
     ELGKGTDLKC VLLVGGDSLE EQFTMMAGNP DIVIATPGRF LHLKVEMNLD LYSIRYVVFD
     EADRLFEMGF AAQLTEILHG LPPNRQTLLF SATLPKSLVE FARAGLQEPT LIRLDTESKI
     SPDLQNAFFS IKSSEKEGAL LYILHEVIKM PTGPTEMAQQ RQGEDASARF SKANKRKRAE
     MEKAVNTKES PTQHSTIVFA ATKHHVDYLY SLLHEAGFAV SYVYGALDQT ARKIQVQNFR
     SGLSNILVVT DVAARGIDIP ILANVINYDF PSQPKIFIHR VGRTARAGRK GWSYSLVRDA
     DAPYLLDLQL FLGRRLVVGR ENGDHVNFAE DVVAGGLPRD GLSQNCEWVT KVLGDDADIA
     AQRTVATKGE KLYMRTRNSA SLESAKRAKQ VVSSDHWTSI HPLFQDESSN LEAEREKMLA
     RIGGYRPSET IFEVNTRRIG KQESEEALNT IKRVRTTLET KKKRSKANAK SEFLEDAPEG
     LKTGEGEAGK NEDEAAFSDA DDIDAPTGVA DDMSLASDSE LEVTFSSYSQ SNGNKSKKAS
     AASFQNPDYF MSYTPNNNSL AEDRAYGVHS GTNSNFAQAS RSATMDLAGD EGSRGFGEPR
     TMMRWDKRHK KYVARQNDED GSKGTRLVRG ESGAKIASSF RSGRFDAWKR GNRVGRMPRV
     GEAEAPNLAA GLNAALSGKR FKHRREQAPK RADPLRGDYE KMKKKADKAK ERSMSKAGGA
     AAGGKSELRN TDDIRIARKL KQRRQEKNAR PSRKR