DBP9_KLULA
ID DBP9_KLULA Reviewed; 594 AA.
AC Q6CUI6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ATP-dependent RNA helicase DBP9;
DE EC=3.6.4.13;
GN Name=DBP9; OrderedLocusNames=KLLA0C04576g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382123; CAH01254.1; -; Genomic_DNA.
DR RefSeq; XP_452403.1; XM_452403.1.
DR AlphaFoldDB; Q6CUI6; -.
DR SMR; Q6CUI6; -.
DR STRING; 28985.XP_452403.1; -.
DR PRIDE; Q6CUI6; -.
DR EnsemblFungi; CAH01254; CAH01254; KLLA0_C04576g.
DR GeneID; 2892335; -.
DR KEGG; kla:KLLA0_C04576g; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; Q6CUI6; -.
DR OMA; GYEKDFK; -.
DR Proteomes; UP000000598; Chromosome C.
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: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..594
FT /note="ATP-dependent RNA helicase DBP9"
FT /id="PRO_0000232343"
FT DOMAIN 47..229
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 242..474
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 562..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..43
FT /note="Q motif"
FT MOTIF 175..178
FT /note="DEAD box"
FT COMPBIAS 562..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 594 AA; 67455 MW; 25E1077C1F05054F CRC64;
MAQTSASQGY IDDSSSFDSF HLDSRLSQAI RSIGFKHPTL IQSSAIPLAL QEKRDIIAKA
STGSGKTLAY LIPVIQTILD HKKADQNDEG ATLGVILVPT RELAQQVLEV VEKLIVFCSQ
EIKCLNLSSG NVSGNLLKSL LTENPEILIA TPAKLVDLLD AQDVNIDRLK FLVIDEVDLV
LTFGYQEDLT KISERLPLRK SLQTFLMSAT LNDDIQHLKQ QFCRSPAILK LNDDEVNKDQ
TKLIQYYVKV GEFDKFLLCY VIFKLGLIKG KTLIFVNNID RGYRLKLVLE QFGIKSCILN
SELPANSRQH IVEEFNKNVY QLLIATDDTE YIKEEDEDLE SEKTEDGLVE VVDDSTVTTK
DNAKKQKKPK LNVEKDKEYG VSRGVDFKNV ACVLNFDLPT TAKSYVHRIG RTARAGKSGI
SISFVVPLKE FGKHKPSMIK SAKKDEKILG RIIKQQAKLG FELQPYNFDI KQVEGFRYRM
EDGFRAVTQV AIREARIKEL KQELLASEKL KRHFEENPHD LESLRHDKEL HPARVQQHLK
RVPDYLLPET ARKDNKKIGF VPFHKNSHRK NGRVVKKKGN VQRKGKSDPL KSFK
