ID   DBP6_CANGA              Reviewed;         651 AA.
AC   Q6FST5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ATP-dependent RNA helicase DBP6;
DE            EC=3.6.4.13;
GN   Name=DBP6; OrderedLocusNames=CAGL0G07975g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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; CR380953; CAG59636.1; -; Genomic_DNA.
DR   RefSeq; XP_446709.1; XM_446709.1.
DR   AlphaFoldDB; Q6FST5; -.
DR   SMR; Q6FST5; -.
DR   STRING; 5478.XP_446709.1; -.
DR   PRIDE; Q6FST5; -.
DR   EnsemblFungi; CAG59636; CAG59636; CAGL0G07975g.
DR   GeneID; 2888250; -.
DR   KEGG; cgr:CAGL0G07975g; -.
DR   CGD; CAL0130153; CAGL0G07975g.
DR   VEuPathDB; FungiDB:CAGL0G07975g; -.
DR   eggNOG; KOG0350; Eukaryota.
DR   HOGENOM; CLU_003041_15_2_1; -.
DR   InParanoid; Q6FST5; -.
DR   Proteomes; UP000002428; Chromosome G.
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:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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; 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.
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..651
FT                   /note="ATP-dependent RNA helicase DBP6"
FT                   /id="PRO_0000232293"
FT   DOMAIN          240..420
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          452..611
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           216..224
FT                   /note="Q motif"
FT   MOTIF           360..363
FT                   /note="DEAD box"
FT   COMPBIAS        8..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   651 AA;  73113 MW;  638F07E53676B3D9 CRC64;
     MFAARFDPTK VVREEPKIIP QKRAIPDDVE SSDSDQDIED GVEVGAVSKE QSGTDVTTTR
     AVDGKSESDS ESESESESDS DDEMNFDMGG SSSSSDDDEV SSKDADVDDD GKHTSVLSRF
     KKTLSIQDKI SALEEANTQD ILEDGEAHDL AQIPQPAVVR DKKLQVKDIS EMKNTAFRDT
     RKVHYDNSMT KSFEEYSDDL TPKLLNNIEK YFSKSTFPIQ TAMLDQYLKL INFTLKTSKK
     NFTRRIGDIL VNASTGSGKT LAYSIPIIQT LSSRTVNKLR VLIILPTKLL INQVFQTMSQ
     LAEGTSLVIT VSKLENSFNE EHKRLLKTEP DIFITTPGRL VDHLTNSSIS LRNLKFLVLD
     EADRLLNQSF QNWIPEVMSK FKSDKFDQMP GSIIKMVFSA TLTTNTEKLN DLQLYNPTLF
     ATDSVKLYNL PPTLQEYQLQ IPSAKSVYKP LYLLKLLEQL SGGKTLVFVR SNESSLKLEV
     LLKSLIKGHM TTLQIVVHSI NSNNSKAENR RLVTDFTKES LPNQTNVLIT TDLMSRGIDI
     ENIANVINYD VPISSQQYVH RCGRTARANK DGKAYNMLVG KGEAQFWKDS IDEDISRDVS
     GCKPISYNDS YNKVHGDENA RTSEPTRDLF TSIDSETSDK YNEILKNLTQ K