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Database: UniProt
Entry: A2QRY2
LinkDB: A2QRY2
Original site: A2QRY2 
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   31-JUL-2019, entry version 82.
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.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   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.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
DR   EMBL; AM270172; CAK40010.1; -; Genomic_DNA.
DR   RefSeq; XP_001392878.1; XM_001392841.1.
DR   SMR; A2QRY2; -.
DR   PaxDb; A2QRY2; -.
DR   PRIDE; A2QRY2; -.
DR   EnsemblFungi; CAK40010; CAK40010; An08g07610.
DR   GeneID; 4983080; -.
DR   KEGG; ang:ANI_1_1084074; -.
DR   HOGENOM; HOG000246455; -.
DR   KO; K14808; -.
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: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   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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    932       ATP-dependent RNA helicase dbp10.
FT                                /FTId=PRO_0000281714.
FT   DOMAIN      121    293       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      360    515       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     134    141       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        90    118       Q motif.
FT   MOTIF       241    244       DEAD box.
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
//
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