ID   DBP10_DEBHA             Reviewed;         932 AA.
AC   Q6BL34;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; OrderedLocusNames=DEHA2F16720g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89469.2; -; Genomic_DNA.
DR   RefSeq; XP_461087.2; XM_461087.1.
DR   AlphaFoldDB; Q6BL34; -.
DR   SMR; Q6BL34; -.
DR   STRING; 4959.XP_461087.2; -.
DR   PRIDE; Q6BL34; -.
DR   EnsemblFungi; CAG89469; CAG89469; DEHA2F16720g.
DR   GeneID; 2903098; -.
DR   KEGG; dha:DEHA2F16720g; -.
DR   VEuPathDB; FungiDB:DEHA2F16720g; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; Q6BL34; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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..932
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000232314"
FT   DOMAIN          128..300
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          369..529
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           97..125
FT                   /note="Q motif"
FT   MOTIF           248..251
FT                   /note="DEAD box"
FT   COMPBIAS        24..38
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..890
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..922
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141..148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   932 AA;  106230 MW;  6036FC618110DDD1 CRC64;
     MSDEEDYDIA GTLALAGSDS EPESDLNSDN EEVQDEIVSD EDDTKHKPNK KQKLEKGKSK
     QTFPSLELSD DEAENESKDM ASYFVANNPQ AKKAKNGSFP SFGFSKFLLT NISKKGFKQP
     TPIQRKTIPL IMENRDVVGM ARTGSGKTAA FTLPLVEKLK SHSPRVGVRA IILSPSRELA
     SQTFKQVKEF SKGTDLRSIV LIGGDSLEEQ FSSMMTNPDV IVATPGRFLH LKVEMELELK
     TVEYIVFDEA DRLFEMGFAE QLNELIAALP SSRQSLLFSA TLPRSLIDFA KAGLTNPVLV
     RLDAETKISD QLQMAFFSIK NNEREASLLY VLQEVIKLPL ASPEEVKRYS DMEKRDNGSE
     DEAEDENNNK KKRFKFKKER LPPANMLPSK HSTIIFVPTK HHVEYVTTLL KDAGYLVSYI
     YGTLDQHARK QQLYQFRIGM TSLLVVTDVA ARGIDIPILA NVVNYTLPGS SKIFIHRVGR
     TARAGNSGWA YSIVNEKELP YLLDLELFLG RKVLLTSMHE KKCEMLKTKQ SSNYVEPKVS
     YTDRLVLGSI PRVDIETFQE LYENILRNHY ELSVVKGVAT KGEKLYYRTR QSASQESLKR
     SKEILSTGNW DDQHLLFGPN LEKEKEKFLT QLLNRKSKET VFEFNKKGND RDEDSLVEFM
     HKRRKQIAPI QRRAKEKREL LEKERMAGLT HGIENEILKN DGEIGYSGIT IEADEEELQD
     AFEDADELIE KKKIEKKKSF RDPQYFLSHY APAAVIQDQQ LSLSSSFAND AAKATFDLDN
     DEKLNANKQV MQWDRKKGNY VNAHSTDKKF IIGESGQKIP ATYRSGRFDD WKKQRNLKPT
     KTGAMEANAT NGNDRRFKHK KVASPKLPDK FRDDYHKQKE KVKKAVDSGL KVKGYNKPGQ
     KQELRSTEDI RKAREAKDKK KQKNARPSRK RK