GenomeNet

Database: UniProt
Entry: A2QA23
LinkDB: A2QA23
Original site: A2QA23 
ID   DBP6_ASPNC              Reviewed;         593 AA.
AC   A2QA23;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   31-JUL-2019, entry version 76.
DE   RecName: Full=ATP-dependent RNA helicase dbp6;
DE            EC=3.6.4.13;
GN   Name=dbp6; ORFNames=An01g09920;
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   -!- SUBUNIT: Associated with pre-ribosomal particles. {ECO:0000250}.
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. DDX51/DBP6
CC       subfamily. {ECO:0000305}.
DR   EMBL; AM269980; CAK37175.1; -; Genomic_DNA.
DR   SMR; A2QA23; -.
DR   PaxDb; A2QA23; -.
DR   PRIDE; A2QA23; -.
DR   EnsemblFungi; CAK37175; CAK37175; An01g09920.
DR   HOGENOM; HOG000203294; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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; 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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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    593       ATP-dependent RNA helicase dbp6.
FT                                /FTId=PRO_0000294658.
FT   DOMAIN      157    361       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      407    563       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     170    177       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       121    149       Q motif.
FT   MOTIF       285    288       DEAD box.
SQ   SEQUENCE   593 AA;  64576 MW;  D4DAC674E1310E6B CRC64;
     MKDADDSEEV KEEQAKGTKK GRKSSEPAAT ENDDDKPTKN KFAGILSKFE RSKKARELEK
     TRESTKDEDS TEPTTAEPVI AQGLEPLPQP EAAPEQDEMP TYSSLPPWLA NPLRASAQER
     RKFADLGIDS SLLRVLEDNG YREAFAVQST VIPLLLQGPT NHPGDLCISA ATGSGKTLSY
     VLPLVTALKP LPAPRLRGLI VVPTRELVKQ AREACELCAA GSGLRVASAV GNVAIKDEQR
     ESLPGYVHRS EPNVDILICT PGRLVDHLRY TKGFTLKNLE WLVIDEADRL LNESFQEWVD
     VVMTSLDARK APDAFGFSGN FLSGLGLPIQ SKEPRKVVLS ATMTRDVTKL NSLRLANPKL
     VVIGSDAAAT EDESGGVAPS DEQFTLPPTL EEHTVSVGDG SQKPLYLLRL LLSHIKLETK
     ILVFTKSSES ASRLARLLAL LEPSLSDRIG TIIKSNKSSA SRKTLTAYRR GKISVIIATD
     RASRGLDLRS LTHVVNYDVP ASITTYVHRV GRTARAGQKG SAWTLVAHRE GKWFASQIAK
     GSDGKITRST KVGKVQFKLD NMKEVKARYA SALDLLEKEV KTGGTKASKP SAQ
//
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