DBP3_DEBHA
ID DBP3_DEBHA Reviewed; 527 AA.
AC Q6BZ77;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP-dependent RNA helicase DBP3;
DE EC=3.6.4.13;
GN Name=DBP3; OrderedLocusNames=DEHA2A03454g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
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; CR382133; CAG84444.1; -; Genomic_DNA.
DR RefSeq; XP_456492.1; XM_456492.1.
DR AlphaFoldDB; Q6BZ77; -.
DR SMR; Q6BZ77; -.
DR STRING; 4959.XP_456492.1; -.
DR EnsemblFungi; CAG84444; CAG84444; DEHA2A03454g.
DR GeneID; 2899897; -.
DR KEGG; dha:DEHA2A03454g; -.
DR VEuPathDB; FungiDB:DEHA2A03454g; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_1_5_1; -.
DR InParanoid; Q6BZ77; -.
DR OMA; KKKTHDM; -.
DR OrthoDB; 471730at2759; -.
DR Proteomes; UP000000599; Chromosome A.
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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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..527
FT /note="ATP-dependent RNA helicase DBP3"
FT /id="PRO_0000232177"
FT DOMAIN 148..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 348..497
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 119..145
FT /note="Q motif"
FT MOTIF 266..269
FT /note="DEAD box"
FT COMPBIAS 1..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 527 AA; 58635 MW; 9A5092A27E6F9D38 CRC64;
MSKDHKDKKR KHSDEATEEV EKKTKVSKKE KKDKKEKKEK KDKKEKKDKS EKKDKSEKKE
KKEKKESEDV PTKSSAVVST GYSQSPALTK LPQSEIDSFL QENEVTVEDP HNLGLRPLLG
FDQIDLDSRI ASVISKFPTP TPIQAVSWPY LLSGKDVIGV AETGSGKTFA FGVPAINNIL
THDKKGLKVL CISPTRELAL QIYDNLVDLT ANTPLKCVAV YGGVSKHEQV SSLRNASVVV
ATPGRLIDLL NDGALSLDSI EYLVLDEADR MLEKGFEQDI KSVMQQTNHA NRQTLMFTAT
WPKEVRELAS TFMNSPVKVS IGDRNELSAN KRITQIVEVI EPYDKEKKLL SLLRKYQSGS
NKDDKVLIFA LYKKEATRIE NLLVRNSFKV SAVHGDLSQQ QRTSALGAFK AGKTTLLLAT
DVAARGLDIP NVKVVINLTF PLTVEDYVHR IGRTGRAGQT GIAHTLFTEH EKHLSGALMN
VLRGANQPVP DELLKFGGHT KKKAHSAYGA FFKDVDMTKT AKKIKFD
