DBP7_ASPNC
ID DBP7_ASPNC Reviewed; 771 AA.
AC A2RA55;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase dbp7;
DE EC=3.6.4.13;
GN Name=dbp7; ORFNames=An18g01980;
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 -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; AM270398; CAK47270.1; -; Genomic_DNA.
DR RefSeq; XP_001398657.1; XM_001398620.2.
DR AlphaFoldDB; A2RA55; -.
DR SMR; A2RA55; -.
DR PaxDb; A2RA55; -.
DR PRIDE; A2RA55; -.
DR EnsemblFungi; CAK47270; CAK47270; An18g01980.
DR GeneID; 4989758; -.
DR KEGG; ang:ANI_1_234164; -.
DR VEuPathDB; FungiDB:An18g01980; -.
DR HOGENOM; CLU_003041_26_2_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
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:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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..771
FT /note="ATP-dependent RNA helicase dbp7"
FT /id="PRO_0000281707"
FT DOMAIN 179..378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 403..615
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 23..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..175
FT /note="Q motif"
FT MOTIF 314..317
FT /note="DEAD box"
FT COMPBIAS 23..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 771 AA; 85517 MW; 9C82CB517BF5D3CE CRC64;
MADDGLLLNF AIPDTTVLRP EKTKVKGGTW RDRLSAKKIA AHRTNNPRKE KSASNGEQNS
NPRNPNRIQV SGPRPVKRQR IEDDDGNGGS QPRQQQQQHP GAPRQFVSSL FSKNPRPRNA
VEEKNEAGAE VEDAKPTNAP LIDGLDTFTN LGLSAPLAAH LLTKLEVKAP TAIQKASITQ
LLKEESDAFI QAETGSGKTM AYLLPLVQRI MTISLNQKKR EEGEQVQRDS GLFAIVLAPT
RELCKQIAVV LEGLLRCAHW IVAGTVIGGE KKKSEKARLR KGLNILVATP GRLADHLENT
QALDVSNVRW LVLDEGDRLM ELGFEKELAG IIQKLDARQR PSRIPGIPAK RTTILCSATL
KMTVQKLGEI SLKDAVHIQA DPADEDGEPR KKDEDDAFRV PAQLKQSYAI VASKLRLVTL
TAFMKRTFMR KGSVMKAIIF VSCADSVDFH FEVFTRKNGD EEEKKEESED SDEEDAEEKR
KKLGASAHGT IAPATAFSNP SNPVALHRLH GSLPQHVRTA TLGAFARNRE PSVLICTDVA
SRGLDLPNVD LVVEYDPAFS AEDHLHRIGR TARLGRDGRA LIFLMPGCEE GYVDILKKGY
RDGGKALTRN SADDILKRGF GGNVESQNVD WEEKATEWQL DVERWALENK NYLEMARRAY
QSHIRAYATH IANERSMFNI KELHLGHLAK SFALRDRPSK INVPGLRQAQ ADTKKDFKAD
RKPVAGKKRK AGGHDDDDDD VPRQTDTLTA AQKMRAKMKE HMAGASEFNL A
