GenomeNet

Database: UniProt
Entry: A2RB17
LinkDB: A2RB17
Original site: A2RB17 
ID   RRP3_ASPNC              Reviewed;         467 AA.
AC   A2RB17;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 72.
DE   RecName: Full=ATP-dependent rRNA helicase rrp3 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P38712};
GN   Name=rrp3 {ECO:0000250|UniProtKB:P38712}; ORFNames=An18g05150;
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., 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-dependent rRNA helicase required for pre-ribosomal RNA
CC       processing. Involved in the maturation of the 35S-pre-rRNA and to its
CC       cleavage to mature 18S rRNA. {ECO:0000250|UniProtKB:P38712}.
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         Evidence={ECO:0000250|UniProtKB:P38712};
CC   -!- SUBUNIT: Interacts with the SSU processome.
CC       {ECO:0000250|UniProtKB:P38712}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
DR   EMBL; AM270408; CAK43313.1; -; Genomic_DNA.
DR   RefSeq; XP_001398969.1; XM_001398932.2.
DR   SMR; A2RB17; -.
DR   PaxDb; A2RB17; -.
DR   PRIDE; A2RB17; -.
DR   EnsemblFungi; CAK43313; CAK43313; An18g05150.
DR   GeneID; 4990081; -.
DR   KEGG; ang:ANI_1_682164; -.
DR   HOGENOM; HOG000268802; -.
DR   KO; K14777; -.
DR   Proteomes; UP000006706; Chromosome 8L.
DR   GO; GO:0005634; C:nucleus; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..467
FT                   /note="ATP-dependent rRNA helicase rrp3"
FT                   /id="PRO_0000282695"
FT   DOMAIN          79..250
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          262..422
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         92..99
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           48..76
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           198..201
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  51483 MW;  1CFD10D564338DE3 CRC64;
     MPGVKKRKVA REAPAPAPAQ ESDVESSTPE QTQEPEAQEQ EQEEGQSKTF KELGIIEQLC
     EACETMGYKA PTPIQRESIP LALKGRDLIG LAETGSGKTA AFALPILQAL MEKPQPFFGL
     VLAPTRELAY QISKSFESLG ASMGVRSCVI VGGMDMVSQS ISLGKKPHII VATPGRLLDH
     LENTKGFSLR NLKYLVMDEA DRLLDMDFGP LLDKILKVLP RERRTFLFSA TMSSKVESLQ
     RASLSNPLRV SVSTSKYQTV STLLQSYLFI PQKHKDLYLV YLLNEFAGQS TIIFTRTVNE
     TQRLAFLLRA LGFGAIPLHG QLSQSARLGA LGKFRARSRN ILVATDVAAR GLDIPSVDVV
     LNFDLPGDSP SYVHRVGRTA RAGKSGLAIS FVAQYDVEVW LRIEGALGKK LKEYDCPKDE
     VMVLGENVAE AQRQAIMDMK DYNEKKGSRG KKFGGKRSRD EMDQEEG
//
DBGET integrated database retrieval system