ID   DBP10_ASPOR             Reviewed;         929 AA.
AC   Q2UHC1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=ATP-dependent RNA helicase dbp10;
DE            EC=3.6.4.13;
GN   Name=dbp10; ORFNames=AO090023000504;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007157; BAE59044.1; -; Genomic_DNA.
DR   RefSeq; XP_001821046.1; XM_001820994.2.
DR   AlphaFoldDB; Q2UHC1; -.
DR   SMR; Q2UHC1; -.
DR   STRING; 510516.Q2UHC1; -.
DR   EnsemblFungi; BAE59044; BAE59044; AO090023000504.
DR   GeneID; 5993048; -.
DR   KEGG; aor:AO090023000504; -.
DR   VEuPathDB; FungiDB:AO090023000504; -.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   OMA; MRWDKKS; -.
DR   Proteomes; UP000006564; Chromosome 3.
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..929
FT                   /note="ATP-dependent RNA helicase dbp10"
FT                   /id="PRO_0000232310"
FT   DOMAIN          120..292
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          358..513
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..48
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..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..929
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        12..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..685
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..929
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   929 AA;  103096 MW;  CF433DC2F9F7EB0A CRC64;
     MPHRAASPAA SENEFDITNA LFQNDSDSDN DTSLKQTKRP QKAAPPQALD FLGGDIDDDE
     DDEAFIAGQQ ASANRKASNL KGRTVKKGGG FQAMGLNAHL LKAITRKGFS VPTPIQRKTI
     PVIMDGQDVV GMARTGSGKT AAFVIPMIEK LKSHSTKVGA RGLILSPSRE LALQTLKVVK
     ELGKGTDLKS VLLVGGDSLE EQFSLMAGNP DIVIATPGRF LHLKVEMNLD LSSIRYVVFD
     EADRLFEMGF ADQLTEILYG LPANRQTLLF SATLPKSLVE FARAGLQEPT LIRLDTESKI
     SPDLENVFFS VKSSEKEGAL LHILHEVIKM PTGPTEAAQR QKEQGDGKNF KNFKKRKRGD
     DKAINFQESP TKYSTIVFAA TKHHVDYLYS LLREAGFAVS YAYGSLDQTA RKIQVQNFRA
     GLSNILVVTD VAARGIDIPI LANVINYDFP SQPKIFVHRV GRTARAGRKG WSYSLVRDAD
     APYMLDLQLF LGRRLVIGRE HGDQVNFAED VVVGSLPRDG LSTSCEWVTK VLENEADIYS
     QRTIAGKGEK LYMRTRNSAS LESAKRAKQV VSSDNWTAVH PLFNDQGSQM ELEREKMLAR
     IGGYRPQETI FEVHNRRNGK HEGDEAIDTI KRIRTTVDYK KKKREMAEKQ SDFVEDASSG
     NKGEANETEE TGAQPDEDEE DIGEGVPDNM SMASESDLEV TFSSYNGGKA KKDSAASFQN
     PEYFMSYTPS STNLAEDRAY GVHTGTNANF TQASRSATMD LLGDEGARGF AEPRTMMRWD
     KRHKKYVSRQ NDEDGSKGTH LVKGESGAKI ASTFRSGRFD AWRKGKRLGR MPRVGEEETP
     ALVHDLNTAM RRRRFQHRKE QAPKAADRLR GDYEKMKKKG EAAKQRQLSK AGGAAAGGKS
     ELKSTDDIRL ARKLKQQRRE KNARPSRKK