DBP10_ASPNC
ID DBP10_ASPNC Reviewed; 932 AA.
AC A2QRY2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP-dependent RNA helicase dbp10;
DE EC=3.6.4.13;
GN Name=dbp10; ORFNames=An08g07610;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270172; CAK40010.1; -; Genomic_DNA.
DR RefSeq; XP_001392878.1; XM_001392841.1.
DR AlphaFoldDB; A2QRY2; -.
DR SMR; A2QRY2; -.
DR PaxDb; A2QRY2; -.
DR EnsemblFungi; CAK40010; CAK40010; An08g07610.
DR GeneID; 4983080; -.
DR KEGG; ang:ANI_1_1084074; -.
DR VEuPathDB; FungiDB:An08g07610; -.
DR HOGENOM; CLU_003041_5_0_1; -.
DR Proteomes; UP000006706; Chromosome 8R.
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..932
FT /note="ATP-dependent RNA helicase dbp10"
FT /id="PRO_0000281714"
FT DOMAIN 121..293
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 360..515
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..932
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 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..684
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
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 932 AA; 102626 MW; 93DB74AFA6D8A37A CRC64;
MPGRAASPAM SENEFDITNA LFQNDSDSDN EAPAKQAKRQ PKAAAPQQLD FLNGGGDDDD
EDDEAFIAET QASANRKASN LKGRTVKKGG GFQAMGLNAN LLKAITRKGF SVPTPIQRKT
IPVIMEDQDV VGMARTGSGK TAAFVIPMIQ KLKSHSTQVG ARGLILSPSR ELALQTLKVV
KELGKGTDLK AVLLVGGDSL EEQFSMMAGN PDIVIATPGR FLHLKVEMNL DLSSIRYVVF
DEADRLFEMG FAAQLTEILH GLPSTRQTLL FSATLPKSLV EFARAGLQEP TLVRLDTESK
ISPDLQNAFF SVKSGDKEGA LMYILHNVIK MPTGPTEAAQ RMKEENASGK SSKFSKKRKR
SDDKAINFKE SPTKHSTIIF AATKHHVDYL YSLLNEAGFA TSYAYGSLDQ TARKIQVHNF
RTGISNILVV TDVAARGIDI PILANVINYD FPSQAKIFVH RVGRTARAGR TGWSYSLVRD
SDAPYLLDLQ LFLGRRLVLG REHGDQVNFA EDVVVGGFPR DGLSQSCEWV NKVLDDTVDI
AAQRSVASKG EKLYLRTRNA ASLESAKRSK EVVSSDNWTA LHPLFNDETS QLEAEREKML
ARIGGYRPNE TIFEVNNRRS GKPENEEALT TIKRVRTTLD SKKKRAQEAK SEFVDDDVPT
KSGDADADDA EDGAFSDEDE AGEGAADNMS LASESDLEVT FSSYNQPSNK KAKKEASATS
FQNPEYFMSY TPNNTNMAED RAYGVHSGTN ANFAQASRDA AMDLLGDEGS RGFGEPRTMM
RWDKRHKKYV SRQNDEDGSK GTRLVRGESG AKIAASFRSG RFDAWKKGKR LTRLPRVGEA
ETPGLGADLN HYRGGRRFKH NKEQAPKRAD PLRGDYDKMK KKNEAAKERQ LGKFGGAAAG
GKSELKGTDD IRLARNLKQK RREKNARPSR KK
