ID   DBP10_PICGU             Reviewed;         914 AA.
AC   A5DLR3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=PGUG_04214;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408159; EDK40116.2; -; Genomic_DNA.
DR   RefSeq; XP_001483485.1; XM_001483435.1.
DR   AlphaFoldDB; A5DLR3; -.
DR   SMR; A5DLR3; -.
DR   STRING; 4929.XP_001483485.1; -.
DR   PRIDE; A5DLR3; -.
DR   EnsemblFungi; EDK40116; EDK40116; PGUG_04214.
DR   GeneID; 5125135; -.
DR   KEGG; pgu:PGUG_04214; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; A5DLR3; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000001997; 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..914
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000294667"
FT   DOMAIN          130..302
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          368..522
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           99..127
FT                   /note="Q motif"
FT   MOTIF           250..253
FT                   /note="DEAD box"
FT   COMPBIAS        26..41
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..914
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         143..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   914 AA;  103790 MW;  070EAD2610A6FAC0 CRC64;
     MSDNEYDITN ALALDAGSDS DSDVSSGRED VEDDIQDEII SDDEEKSSSS QNKKPKISTK
     PESFPSLELS DDEDDESRPS EVAEYFSNNK LQATKAKAGS FASFGLSKFL LKNIAKKGFK
     QPTPIQRKTI PLVMESRDVV GMARTGSGKT AAFVLPVVEK LKSHSPKVGV RAVILSPSRE
     LALQTFKQVK EFTKGTDLRS IVLIGGDSLE DQFSSMMTNP DILVATPGRF LHLKVEMNLD
     LKTVEYIVFD EADRLFEMGF AEQLNELLVA LPPSRQSLLF SATLPRSLVD FAKAGLSNPV
     LVRLDAETKI SDQLQMAFFT TKRTERDANL LYILSEVIKM PLATQDQIKK LKELEEGADD
     DDSDEEKKPK KKKRKLEKPA PANRLPSEHS TIVFVPTKHH VEYVTTLLRD AGHLVSYIYG
     TLDQHARKQQ LYQFRAAYTN ILVVTDVAAR GIDIPVLANV VNYTLPGSSK IFIHRVGRTA
     RAGNKGWAYS IVNEKELPYL LDLELFLGKK VLLTQMHEKK VQICHEKGLS APEVSYKDRL
     VLGSAPRVDI ESSQELCDNL LRNHYELRTI RDVANKGEIL YYRTRQPASQ ESVKRAKEIM
     DTGAWDDQHL LFGANLEKEK EKFLAKLADR KVKETVFEFR NKGQRDEDSL VEFMHKRRRQ
     IAPIQRRAKE RKQLLEKERM AGLTHGIENE ILKGDGEVGY DNYNGADLDE VFEDGDEALS
     KKKRKTYRDP QFFLSHYAPA SVIQDKQLEL SSFSNEAAAA TYDLDNDDKT QTNKQIMRWD
     KKKGKYINSQ STDKKYIIGE SGQKIPATYR SGRYEDWRKS RNAQPLRTGA EEVKSNGRFK
     HKKVAAPKMP DKFRDDYHKQ KKKVEKALDA GVSVKGYNRP GQQQELRSTE QIRKARELKE
     KRKAKNARPS KRRK