ID   DBP1_CANGA              Reviewed;         604 AA.
AC   Q6FP38;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ATP-dependent RNA helicase DBP1;
DE            EC=3.6.4.13;
GN   Name=DBP1; OrderedLocusNames=CAGL0J06908g;
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 translation initiation.
CC       Remodels RNA in response to ADP and ATP concentrations by facilitating
CC       disruption, but also formation of RNA duplexes. Redundant to DED1, may
CC       be required in conditions in which DED1 expression is decreased (By
CC       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: Cytoplasm {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. DDX3/DED1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR380956; CAG60957.1; -; Genomic_DNA.
DR   RefSeq; XP_448006.1; XM_448006.1.
DR   AlphaFoldDB; Q6FP38; -.
DR   SMR; Q6FP38; -.
DR   STRING; 5478.XP_448006.1; -.
DR   EnsemblFungi; CAG60957; CAG60957; CAGL0J06908g.
DR   GeneID; 2889622; -.
DR   KEGG; cgr:CAGL0J06908g; -.
DR   CGD; CAL0133642; CAGL0J06908g.
DR   VEuPathDB; FungiDB:CAGL0J06908g; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   InParanoid; Q6FP38; -.
DR   OMA; NHGNSRL; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; 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   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; 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; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..604
FT                   /note="ATP-dependent RNA helicase DBP1"
FT                   /id="PRO_0000255988"
FT   DOMAIN          169..358
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          386..529
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           138..166
FT                   /note="Q motif"
FT   MOTIF           302..305
FT                   /note="DEAD box"
FT   COMPBIAS        34..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         182..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   604 AA;  66715 MW;  B7DF84C2855B3288 CRC64;
     MSDGSGRYVP PHIRRGGGNS HESAAADGLS GSRYSGNGFF SSPNRGNHKS SGGFFGSRPF
     NDRRTGQGSR ASGSGGFGGS GGRYGWVNGK HVPYPKNPRL EMELFGNATD HVTSGINFDN
     YDDIPVEASG DNVPEAITEF KSPPLDELLL ENVELANFSK PTPVQKYSIP IVTKNRDLMA
     CAQTGSGKTG GFLFPVLSEL FLNGPAPLPE HTRHSYMRKC YPSALVLAPT RELAIQIFDE
     AKKYTYRSWV KPYVVYGGAP IGQQMRDMDR GCNLLVATPG RLNDLLERGK ISLVNVKYLV
     LDEADRMLDM GFEPQIRHIV EDCDMPSVND RQTLMFSATF PREIQHLARD FLKDYIFLSV
     GRVGSTSENI QQKVLFVEDY DKNSALLDIL INEIDGLTLV FVETKRMADQ LTDFLIVQNF
     KATAIHGDRT QAERERALHA FRNGIANILV ATAVAARGLD IPNVTNVINY DLPTDIDDYV
     HRIGRTGRAG NVGVATSFFN SNSMNIAKEL MDLLTEANQE VPQFLVNMVQ DSMRFGRGGR
     NSRTGSNRGR GSNTRDYRHS NKDDWGSLGS SRRGFRSNDN RGFGNNWGSS SGDGFTNKAA
     NSWW