DBP9_ASPCL
ID DBP9_ASPCL Reviewed; 621 AA.
AC A1C7F7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP-dependent RNA helicase dbp9;
DE EC=3.6.4.13;
GN Name=dbp9; ORFNames=ACLA_073630;
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. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; DS027045; EAW14328.1; -; Genomic_DNA.
DR RefSeq; XP_001275754.1; XM_001275753.1.
DR AlphaFoldDB; A1C7F7; -.
DR SMR; A1C7F7; -.
DR STRING; 5057.CADACLAP00006759; -.
DR EnsemblFungi; EAW14328; EAW14328; ACLA_073630.
DR GeneID; 4707837; -.
DR KEGG; act:ACLA_073630; -.
DR VEuPathDB; FungiDB:ACLA_073630; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR OMA; GYEKDFK; -.
DR OrthoDB; 973872at2759; -.
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: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..621
FT /note="ATP-dependent RNA helicase dbp9"
FT /id="PRO_0000281717"
FT DOMAIN 58..236
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 247..489
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 342..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..621
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 342..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..621
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 621 AA; 69531 MW; 906A244C7075B5E7 CRC64;
MKRKLDANDV PSAEVAEGKE AKDADNTDFE NLNLDPRLRQ ALIKEQFTKP TPVQSKAIPL
ALEGKDILAR AKTGSGKTAA YVLPILQTIL QKKAADPSLK ATTGLILVPT RELAEQVQSV
ITKFTAFCGK DVRSVNLTQK VSDAVQRTML ADYPDLIVST PARVIANLGS SALALDNLTH
LVIDEADLVL SYGYDEDINA LAKAIPRGVQ TFLMSATLTS EVDTLKGLFC RNPVVLKLED
KEDEGAGISQ FVVRCAEDEK FLLTYVIFKL QLIKGKVIIF VGDIDRCYRV KLFLEQFGIK
SCVLNSELPI NSRIHVVQEF NKGVYDIIIA ADEQEVMGAR TTFKKSKEIT DGDEEETRDK
MGSSEDEDNE PEDNDKKSAH PEKRRKTSGK GKDYGISRGI DFQNVACVLN FDLPTTSKSY
THRIGRTGRA GKAGMALSFV VPADEFGKHK PTSFPTAKYD ESVLAKIVKR QAKLDHEVKP
YHFEMKQVDA FRYRMTDALR SVTRLAIQEA RAREIRQELV KSEKLKRHFE ENPEELKQLR
HDGELRAARI QPHLKHIPDY LMPSKGRKGI SSENVGYVGF TKQSDNRIRK AREKNRGKGK
GRKPSGVRKV DPLKTFNRGR K
