ID   DBP10_YARLI             Reviewed;         926 AA.
AC   Q6C7X8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; OrderedLocusNames=YALI0D24497g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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   -!- 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; CR382130; CAG81435.1; -; Genomic_DNA.
DR   RefSeq; XP_503234.1; XM_503234.1.
DR   AlphaFoldDB; Q6C7X8; -.
DR   SMR; Q6C7X8; -.
DR   STRING; 4952.CAG81435; -.
DR   EnsemblFungi; CAG81435; CAG81435; YALI0_D24497g.
DR   GeneID; 2910446; -.
DR   KEGG; yli:YALI0D24497g; -.
DR   VEuPathDB; FungiDB:YALI0_D24497g; -.
DR   HOGENOM; CLU_003041_5_0_1; -.
DR   InParanoid; Q6C7X8; -.
DR   OMA; MRWDKKS; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; 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; 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; 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..926
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000232320"
FT   DOMAIN          133..305
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          370..529
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          362..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           102..130
FT                   /note="Q motif"
FT   MOTIF           253..256
FT                   /note="DEAD box"
FT   COMPBIAS        24..46
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         146..153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   926 AA;  102850 MW;  1FEC413E60789D53 CRC64;
     MSDSEVEYDI AGSLNPGVDS EDDYSSGSES DSEIPDIIED SEDETGPQQG EPGTMTFPNL
     ELSDDDDDDD DDDEGRKKKK KKTDDSVESY FGAPQTGKKS SGSFAGLGLS QLVLKNIARK
     GFKQPTPIQR KTIPLVLEGK DVVGMARTGS GKTAAFVLPM LEKLKVHSAK VGARAVILSP
     SRELALQTLK VVKDFSAGTD LRLAMLVGGD SLEEQFKMMM SNPDIIIATP GRFLHLKVEM
     ELSLASVEYI CFDEADRLFE LGFGEQMNEL LASLPSNRQT LLFSATLPKT LVEFAKAGLH
     DPILVRLDAE TKLPEHLEMT FFAVKENQRD ACLAFILKEV IQMPFATPEQ LKELERLDER
     AIDDGERDED RKQKRPKFKK ERLPPAHQLP SEKSTIVFCP TKHHVEYVIV LLQTLGYAVS
     YIYGTLDQHA RKNQLYRFRT GKTSILVVTD VAARGIDVPV LANVINYSLP PSPKVFIHRV
     GRTARAGNRG WAYSIIKDND IPYLLDLEVF LGRKLLTPRL FKQQNPDPSA EPDYVNTLTI
     GAPPRQALEI HGEELAQMVK DSYELQQLSE VAVKGERMYN KTKGSASQES AKRSKQIMAL
     GWDDHHLMFG EDGESAKDAL LARLGQKRIR ETVFEFRKSK TTSGAEMMAT RRAQLAPIQR
     RAAEKRAIQE KERLAGLVHS QDAEIARSTE EDMATEADLT GFTTEEDLRA AKKAQKSKKR
     SFRDSENFMS HYAPTNDDKG YAVGNFAGAA SNATFDLIND GSEMQQKQGM KWDKKKGKFI
     NAGSEGGKKF IRGEGGQRIA ASFRSGRFDK WKAAHKVGNL KVGALEESGP ATKRVLSARE
     FKHNKNEAPK RADKYRDDFH KQKTKVAAAK EDGRIQKPQP KSELKSTADV RKSRILAEKR
     KQKNARPSRG GRGGGRGGRG GGRGGR