ID   DBP10_ASHGO             Reviewed;         960 AA.
AC   Q757U8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; OrderedLocusNames=AEL086W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52599.1; -; Genomic_DNA.
DR   RefSeq; NP_984775.1; NM_210129.1.
DR   AlphaFoldDB; Q757U8; -.
DR   SMR; Q757U8; -.
DR   STRING; 33169.AAS52599; -.
DR   EnsemblFungi; AAS52599; AAS52599; AGOS_AEL086W.
DR   GeneID; 4620965; -.
DR   KEGG; ago:AGOS_AEL086W; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_2_1; -.
DR   InParanoid; Q757U8; -.
DR   OMA; MRWDKKS; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
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   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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..960
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000227952"
FT   DOMAIN          151..323
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          388..546
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           120..148
FT                   /note="Q motif"
FT   MOTIF           271..274
FT                   /note="DEAD box"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..960
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   960 AA;  108044 MW;  4500982346D7568F CRC64;
     MGLASKRKRD TEEHSDEGED FDIAGNIALD SEDSDDSVSD SDNEVQDIIE FSDDEKQNAP
     QVSKTAKGAK GAKVAAPRSD AAFPSLELSD GEDADNGDKD DVDSYFNTTS QLAASKAKKG
     SFASFGLSKF ILGNISRKGF RQPTPIQRKT IPLILQQRDI VGMARTGSGK TAAFVLPLIE
     KLKMHSAKIG ARAMILSPSR ELAMQTHKVF KEFAKGSNLR SVLLTGGDGL EDQFSMMMSN
     PDVIIATPGR FLHLKVEMNL DLHSIEYVVF DEADRLFEMG FQEQLNELLG SLPTARQTLL
     FSATLPSSLV DFAKAGLTNP VLVRLDTETK VSENLEMLFL SVKNDEREAN LLYLLQEVIK
     IPVATEEQLQ RFRKQSNDDA DDSDDETDKK KKHSKKSKQP LPSAKDMPSP NSTIIFVSTR
     HHVEYVSNLL KDCGYLVSYL YGTLDQHARR QQLHNFRCGL TNILVVTDVA ARGVDIPLLA
     NVVNMSLPAS SKIFVHRVGR TARAGNKGWA YTILSESELP YLLDLELFLG KKVLLTPMYE
     ATCDLLKKKW ISEGNEGALF QPPKISYVNR LILGSAPRLD LEAMGDLFKN LVESNFELQN
     LKAVSIKAEK LYLRTRQPAS AESIKRAKEV IAAGWDEQNV RFGKNIEKEK LEFLAKLQNR
     HNKETVFEFA RNHDDEMAIL MKRRRRQIAP IQQRAKERQQ LLEKERQAGL RHTLEDEILK
     GEENEVGYSV PQELLRDFED ADELAAKRNT KKGFRDENFY LSHFAPASDI QDKQLQVASS
     FTNEVSKATF DLHNDDKVQV HKQTATVKWD KKRKKYVNVQ GIDNKKYIIG ESGQKIPASF
     RSGKFDEWSK ARKLAPLKVG ARESSIPANL LADPTGSRLA NGKFKHKQIK APKMPDKNRD
     DYQSQLKKVN KAMESGLHVK GYNAPGMKQE LRTTEQIRKQ RSMAEKRKAK NARPAKKRKF