DBP9_ASPOR
ID DBP9_ASPOR Reviewed; 605 AA.
AC Q2UFL0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ATP-dependent RNA helicase dbp9;
DE EC=3.6.4.13;
GN Name=dbp9; ORFNames=AO090026000163;
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. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; AP007159; BAE59655.1; -; Genomic_DNA.
DR RefSeq; XP_001821657.1; XM_001821605.1.
DR AlphaFoldDB; Q2UFL0; -.
DR SMR; Q2UFL0; -.
DR STRING; 510516.Q2UFL0; -.
DR PRIDE; Q2UFL0; -.
DR EnsemblFungi; BAE59655; BAE59655; AO090026000163.
DR GeneID; 5993685; -.
DR KEGG; aor:AO090026000163; -.
DR VEuPathDB; FungiDB:AO090026000163; -.
DR HOGENOM; CLU_003041_17_1_1; -.
DR OMA; GYEKDFK; -.
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:0003678; F:DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-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; 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; 2.
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..605
FT /note="ATP-dependent RNA helicase dbp9"
FT /id="PRO_0000232336"
FT DOMAIN 58..236
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 247..469
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..55
FT /note="Q motif"
FT MOTIF 184..187
FT /note="DEAD box"
FT COMPBIAS 359..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 605 AA; 67887 MW; BE1C3B1C8B7CC1C6 CRC64;
MKRKLDANDV PSPEAADKKE KKEEDDADFE SLNLDPRLRQ ALIKEKFTKP TLVQAKAIPL
ALEGKDILAR AKTGSGKTAA YVLPILQTIL QKKATDPSFK ATTGLILVPT RELAEQVQNV
VTTFAAFCGK DVRSVNLTQK VSDAVQRTML ADYPDLVVST PARVVTNLGS SALSLENLTH
LVIDEADLVL SYGYEEDINA LAKAIPRGVQ TFLMSATLTD EVDTLKGLFC RSPVTLKLED
KDDQGAGVSQ FVVRCAEDEK FLLTYVIFKL QLIKGKVIIF VDDVDRCYRV KLFLEQFGIK
SCVLNSELPI NSRIHVVQEF NKGVYDILIA ADEQEVIGAR KSKKSKETEE AGSSDEDEGE
PEDKSKRRKV SGKEKDYGIS RGIDFQNVAC VLNFDLPSTS KSYTHRIGRT GRAGKTGMAL
SFVIPKDQHG KHRPTSTATS KHDESVLAKI VKRQGKLGHE VKPYHFEMKQ VEAFRYRMTD
ALRAVTRLAV QEARAREIRQ ELIKSEKLKR HFEENPEELR QLRHDDELRS ARVQPHLKHI
PEYLMPAKGK KGLSSGDVGF VSFRKQNENR IRKAREKNRG KGNGRKFAGV KKKVDPLKTF
NRGRK
