DBP9_ASHGO
ID DBP9_ASHGO Reviewed; 595 AA.
AC Q74ZC1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent RNA helicase DBP9;
DE EC=3.6.4.13;
GN Name=DBP9; OrderedLocusNames=AGR278C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; AE016820; AAS54768.1; -; Genomic_DNA.
DR RefSeq; NP_986944.1; NM_212006.2.
DR AlphaFoldDB; Q74ZC1; -.
DR SMR; Q74ZC1; -.
DR STRING; 33169.AAS54768; -.
DR EnsemblFungi; AAS54768; AAS54768; AGOS_AGR278C.
DR GeneID; 4623246; -.
DR KEGG; ago:AGOS_AGR278C; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; Q74ZC1; -.
DR OMA; GYEKDFK; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0033677; F:DNA/RNA helicase activity; 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: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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
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; 2.
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..595
FT /note="ATP-dependent RNA helicase DBP9"
FT /id="PRO_0000227951"
FT DOMAIN 48..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 246..479
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 340..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..44
FT /note="Q motif"
FT MOTIF 179..182
FT /note="DEAD box"
FT COMPBIAS 568..583
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 595 AA; 67582 MW; 38DDCEBA2CBF5C21 CRC64;
MSQQTTASSE YLDESKTFSS FQLDLRLQQS LKSSGFHHPT LIQSSAIPLA LEQKRDIIAK
ASTGSGKTLA YLIPVVQTIL EHKSTQGADR TTGTLGVVLV PTRELAQQVR VVLEKLVLYC
SKDIRLLNIS ANVDDSVLGP LLAENPEIII STPSQLVKIL EGKHLQTISL RDLRFLVIDE
VDLILTFGYQ EDLLKISQYL PLKKNLQAFL MSATLNEEIQ ELKTKFCRSP AILKLNDDEI
NKNKNKLLQY YVKVSEFDKF LLCYVIFKLS LIKGKTIIFV NTIDRGYRLK LVLEQFGIRS
CILNSELPLN SRQHIVDEFN KNVYQLLIAT DDNEYIEEED EETVEAGEEG SEKLEEGGEK
LEEITSKTSS TNGKQKIAKK DKEYGASRGV DFQNVSCVLN FDLPTTAKSY VHRIGRTARA
GKSGTAISFV VPLKEYGKHK PSMLVTAKKD EKILARVIKQ QSKLGFQIEP YNFDVKQIEG
FRYRMEDGFR AVTQVAVREA RVKELKQELL ASEKLKRHFE ENPHDLDSLR HDKELHPARV
QQHLKRVPDY LLPEAARETG KKIGFVPFHN PKKNRKGKVA KRKPGRKSDP LKNFK
