DBP6_DEBHA
ID DBP6_DEBHA Reviewed; 576 AA.
AC Q6BPT8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=ATP-dependent RNA helicase DBP6;
DE EC=3.6.4.13;
GN Name=DBP6; OrderedLocusNames=DEHA2E10912g;
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-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 -!- SUBUNIT: Associated with pre-ribosomal particles. {ECO:0000250}.
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. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382137; CAG88021.2; -; Genomic_DNA.
DR RefSeq; XP_459782.2; XM_459782.2.
DR AlphaFoldDB; Q6BPT8; -.
DR SMR; Q6BPT8; -.
DR STRING; 4959.XP_459782.2; -.
DR EnsemblFungi; CAG88021; CAG88021; DEHA2E10912g.
DR GeneID; 2902828; -.
DR KEGG; dha:DEHA2E10912g; -.
DR VEuPathDB; FungiDB:DEHA2E10912g; -.
DR eggNOG; KOG0350; Eukaryota.
DR HOGENOM; CLU_003041_15_2_1; -.
DR InParanoid; Q6BPT8; -.
DR OMA; INIAYIN; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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; 2.
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..576
FT /note="ATP-dependent RNA helicase DBP6"
FT /id="PRO_0000232294"
FT DOMAIN 172..359
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 396..553
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 130..158
FT /note="Q motif"
FT MOTIF 292..295
FT /note="DEAD box"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 576 AA; 65369 MW; 74E324F3F434C17F CRC64;
MSSDTEEASE EIEGNQNQHV NKQPENDDKM DIVEDEETPE EPIENDPNYM SKHHSVFQKF
KSSVHDVKGE EVDEETPEEK EDIEMQDLVP LPQPELPRDK RLVSTAAHLN NLDWLTTPIY
TAPEETKPFA EFQNPPLSSL MIKNLRNMGF ESAFSVQISV LNLMLKDIER NRLQPDMRGD
LLVNASTGSG KTLAYSIPII ESLQTVKVPR VRAIILVPTK PLINQVKTTL NQLSKGTNLS
IVSLKNDLSI KEEGIKLQTN EPDIIVSTPG RLVDHLTNGY ISLKNLQYLV IDEADRLLNQ
SFQNWCQILI SKIDEFTNIK ERNISNSWKL NVQKMIFSAT LTTDAGKLSL LKFHKPRLII
VNNKEQLVNE MFSLPATLNE FKLQFGSAKS SLKPLILSKF LLSKNKLANV LIFTKSNDAS
LRLSRLLSLI MNKLGSETIN IAYINSTNNT TSVRSKILKD FSKQTINILV ATDLIARGID
ILSITDVINY DLPNSSREYV HRVGRTARAN QEGFAYNFCF GKGEAKWFKK LMAQVGRSEK
NIEELELDTK QLIEDNDESM YKESLDELQQ QVFNRA
