GenomeNet

Database: UniProt
Entry: A2QUY7
LinkDB: A2QUY7
Original site: A2QUY7 
ID   DBP5_ASPNC              Reviewed;         482 AA.
AC   A2QUY7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   13-NOV-2019, entry version 74.
DE   RecName: Full=ATP-dependent RNA helicase dbp5;
DE            EC=3.6.4.13;
GN   Name=dbp5; ORFNames=An10g00360;
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-dependent RNA helicase associated with the nuclear
CC       pore complex and essential for mRNA export from the nucleus. May
CC       participate in a terminal step of mRNA export through the removal
CC       of proteins that accompany mRNA through the nucleopore complex.
CC       May also be involved in early transcription (By similarity).
CC       {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: Associates with the nuclear pore complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear
CC       pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Note=Nuclear pore complex cytoplasmic fibrils. {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. DDX19/DBP5
CC       subfamily. {ECO:0000305}.
DR   EMBL; AM270213; CAK49126.1; -; Genomic_DNA.
DR   RefSeq; XP_001402429.1; XM_001402392.2.
DR   SMR; A2QUY7; -.
DR   PaxDb; A2QUY7; -.
DR   PRIDE; A2QUY7; -.
DR   EnsemblFungi; CAK49126; CAK49126; An10g00360.
DR   GeneID; 4990289; -.
DR   KEGG; ang:ANI_1_32174; -.
DR   HOGENOM; HOG000268797; -.
DR   KO; K18655; -.
DR   Proteomes; UP000006706; Chromosome 5EL.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:EnsemblFungi.
DR   GO; GO:0005844; C:polysome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; 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:0008186; F:RNA-dependent ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR   GO; GO:0006409; P:tRNA export from nucleus; IEA:EnsemblFungi.
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; Cytoplasm; Helicase; Hydrolase;
KW   Membrane; mRNA transport; Nuclear pore complex; Nucleotide-binding;
KW   Nucleus; Protein transport; Reference proteome; RNA-binding;
KW   Translocation; Transport.
FT   CHAIN         1    482       ATP-dependent RNA helicase dbp5.
FT                                /FTId=PRO_0000281703.
FT   DOMAIN      107    280       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      291    464       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     120    127       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        74    102       Q motif.
FT   MOTIF       227    230       DEAD box.
SQ   SEQUENCE   482 AA;  53088 MW;  4F97A114BAAE8209 CRC64;
     MASEQPEAGS LADRITKPEE PAPAEAPEQT EDIPQTDGAA AQQGGSDLHE PDYTVEVKLS
     DLQADPNNPL FSVKNFEDLG LDPRILQGLS AMNFRKPSKI QERALPLLLG NPAKNLVGQS
     QSGTGKTAAF VLNILSRLDL SSEQLQKTPQ ALILAPTREL ARQIVGVIQV MGQFLDGLVI
     GTAVPADTGA RPAKMECSVV VGTPGTVMDM IKRRIMIANK LRVLVLDEAD NMLDQQGLGD
     QCIRVKALLP RDIQVVLFSA TFPAHVHEYA SKFAPQANEI TLQHEELTVE GIKQLYLDCS
     NDEDKYQTLV NLYGLLTVGS SIIFVKTRAS AQEIEKRMVA EGHTVASLTG GIEGSQRDAV
     IDQFRAGHAK VLITTNVLAR GIDVSTVSMV INYDIPEIHQ PGARQRQADF QTYLHRIGRT
     GRFGRVGVSI SFVSNREEWE MLNQIQRYFN TNIQRIDTKD WDEVEEIIKK TIKSSRAQLG
     FR
//
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