DBP3_KLULA
ID DBP3_KLULA Reviewed; 504 AA.
AC Q6CT46;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent RNA helicase DBP3;
DE EC=3.6.4.13;
GN Name=DBP3; OrderedLocusNames=KLLA0C15499g;
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-dependent RNA helicase required for 60S ribosomal subunit
CC synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC site A3, which is necessary for the normal formation of 25S and 5.8S
CC rRNAs (By similarity). {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382123; CAH01744.1; -; Genomic_DNA.
DR RefSeq; XP_452893.1; XM_452893.1.
DR AlphaFoldDB; Q6CT46; -.
DR SMR; Q6CT46; -.
DR STRING; 28985.XP_452893.1; -.
DR EnsemblFungi; CAH01744; CAH01744; KLLA0_C15499g.
DR GeneID; 2892034; -.
DR KEGG; kla:KLLA0_C15499g; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_1_5_1; -.
DR InParanoid; Q6CT46; -.
DR OMA; KKKTHDM; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S 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; IPR000629; RNA-helicase_DEAD-box_CS.
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 Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..504
FT /note="ATP-dependent RNA helicase DBP3"
FT /id="PRO_0000232180"
FT DOMAIN 123..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 325..474
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..120
FT /note="Q motif"
FT MOTIF 243..246
FT /note="DEAD box"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 504 AA; 56613 MW; BAF2813F0BF482EB CRC64;
MSKDELKDKK RKVEDEELKS KKKLKKDKKD KKDKKDKKDK KDKKEKKEKK EKKDKKSETE
SFAASASQSD IDEFLKENEV TVSDPSGSNI VPYLDFSQVS FIDQIQKEIS KFPKPTPIQA
VSWPYLLAGK DVIGIAETGS GKTFAFGVPA INNIVTSGDK SSSVKVLVIS PTRELASQIY
DNLIVLTDAC GLRSCCVYGG VPKDQQREDL RRSQVVVATP GRLLDLIEEG SVDLSHVNYL
VLDEADRMLE KGFEEDIKKI IRQTRSTSRQ TLMFTATWPK EVRELASSFM SEPVKVSIGN
RDELSANKRI TQIVEVVDPF RKEKKLLELL KKYHSGPTKN DKVLIFALYK KEASRVERNL
KYNGYDVAAI HGDLSQQQRT QALNEFKAGK CNLLLATDVA ARGLDIPNVK TVINLTFPLT
VEDYVHRIGR TGRAGQYGTA HTLFTEQEKH LAGALVNVLN GAGQPVPEEL KKFGTHTKKK
EHSAYGAFFK DVDLSKKPKK ITFD
