ID   DBP10_LODEL             Reviewed;         948 AA.
AC   A5DZT7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=LELG_02874;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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   -!- 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. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH981526; EDK44695.1; -; Genomic_DNA.
DR   RefSeq; XP_001526316.1; XM_001526266.1.
DR   AlphaFoldDB; A5DZT7; -.
DR   SMR; A5DZT7; -.
DR   STRING; 379508.A5DZT7; -.
DR   EnsemblFungi; EDK44695; EDK44695; LELG_02874.
DR   GeneID; 5233596; -.
DR   KEGG; lel:LELG_02874; -.
DR   VEuPathDB; FungiDB:LELG_02874; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_2_1; -.
DR   InParanoid; A5DZT7; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10.
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   PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 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..948
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000294665"
FT   DOMAIN          152..323
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          395..552
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           121..149
FT                   /note="Q motif"
FT   MOTIF           271..274
FT                   /note="DEAD box"
FT   COMPBIAS        31..60
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..907
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..948
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   948 AA;  107908 MW;  E71E4D9E41657C46 CRC64;
     MTMSDIEDSD VENYDIAGKL ALRSDDELGS DDEQNTSGEE GEEVELQDEI VSSDDDDDDG
     DKGKDTGKMP PTKKAKLDRK PGSDFDFASL DFEAEDNEEE DKTLSSILAL SNPTAKKAKA
     GSFASFGFSK FLLANIAKKG YKQPTPIQRR SIPLIIDNRD VVGMARTGSG KTAAFVLPLI
     EKLKLRSPSG VRAVILSPSR ELALQTYKQV KEFSHGTNLQ SIVLIGGDSL EEDFGKMMTK
     PDIIVCTPGR FLHLKVEMQY DLMSVQYIVF DEADRLFEMG FAEQLNELLL ALPSNRQSLL
     FSATLPRSLV EFAKAGLTNP VLVRLDADSK LSENLQMAYF TTKRNEREAN LLYILQEVIK
     MPLGTPEEVK KLAAMDKRSI ESDEENEEAK EQNNGKKRKY KFKKERMPSA KELPSEKSTI
     IFVPTKHHVE YVTSLLKDAG YLVSYIYGTL DQHARKNQLY LFRIGLTKIL VVTDVAARGI
     DIPVLANVIN FTLPGSSKIF IHRVGRTARA GNKGWAYSIV NSSELPYLLD LEIFLGKKLL
     LTSMHEAKCE LLKKKQGGSF IPPRINYTER LVVGAIPRLD LETFQELYEN LLRNNYEIKV
     LKDVAAKGEK LYHRTRQPAS QESLKRSKEI LETNSWDDQH LLFGENLEKM KDDFLAKLQN
     RNVKETVFEL KKKGVKENDS LAEFMHRRRR QLAPIQRKAQ ERKELLQKER LAGLSHGIEE
     EVLKIDGEAS GYNQNVDEAE LQETFELGDE AHNKKKTFKD PQFFMSHYAP ASVIQDQQLS
     IASSFANDAQ AATFDLDNDD KLQKNKQQVM KWDKKKGKYI NSMSTDKKYI ISENGTKIPA
     TFRSGKFDEW RKQRNLKPTS SLTNNETPEN NKRFKHKKQS VPKLPDKYRD DYHKQKQKVE
     KALDSGMRVK GYNKPGMQQE LKSTEQIRKA RAIKEQRRAK NARPSRRK