ID   DBP10_KLULA             Reviewed;         973 AA.
AC   Q6CIR0;
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=KLLA0F24684g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98887.1; -; Genomic_DNA.
DR   RefSeq; XP_456179.1; XM_456179.1.
DR   AlphaFoldDB; Q6CIR0; -.
DR   SMR; Q6CIR0; -.
DR   STRING; 28985.XP_456179.1; -.
DR   EnsemblFungi; CAG98887; CAG98887; KLLA0_F24684g.
DR   GeneID; 2895208; -.
DR   KEGG; kla:KLLA0_F24684g; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; Q6CIR0; -.
DR   OMA; MRWDKKS; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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   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..973
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000232317"
FT   DOMAIN          157..329
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          408..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          376..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           126..154
FT                   /note="Q motif"
FT   MOTIF           277..280
FT                   /note="DEAD box"
FT   COMPBIAS        378..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   973 AA;  110014 MW;  B5C936A83B68584D CRC64;
     MVDSSKRALP AEDYSSEDED AFDIAGDIAL NADSEDSDIS DDDNDNIGFQ AEVQDVIEFS
     SDEEEKEKKP KKQNKKAKVK AGPIVDSKFP SLELSDDEKK ATNESDDDLN DYFNTTADAA
     AKHKKGSFAS FGLSKLVLIN ISKKGFRQPT PIQRKTIPLI LQKRDIVGMA RTGSGKTAAF
     VLPMIEKLKT HSAKIGVRAV ILSPSRELAI QTHRVFKEFS KGSDLRSILL TGGDSLEDQF
     GMMMGNPDVV IATPGRFLHL KVEMNLDLKS VEYVVFDEAD RLFEMGFQEQ LNELLVAFPT
     NRQTLLFSAT LPSSLVDFAK AGLSNPVLVR LDAETKISEN LEMLFISIKK DEREANLLYL
     LQEAIKMPVA TESQIKKLKQ QNDADSDSDD SEDEKKKKAK KAKKSKRRLP NANEMPSEKA
     TIVFVPTRHH VEYVTQLLKN CGYLVSYIYG ALNQHARKQQ LYNFRAGLTS ILVVTDVAAR
     GVDIPLLANV INYSLPGSSK IFIHRVGRTA RAGNRGWAFS IVSENELPYL LDLELFLGKK
     ILLTPMYESS CQILRKKAES EGNNNFTDPK VSYTTRMVLG ACPRSEIDGM GDLYSNMIKS
     DFELNTVKGV ALKAEKLYFR TRTPASAESM KRSKEILRSG WDEQNIYFGK NAEKEKLDFL
     AKLQHRNNKE TVFEFARNPD DEMSVLMKRR RRQIAPIQRK AKERQELLEK ERMIGLRHSI
     EDEILKGEDN EVGYSVPDEV LKEFEDADVL LEEQENIKKK QKKTFRDPTF YLSHFAPTSD
     IQDKQLQISS GFTNDASNAA FDLANDDKVQ VHKQTATVKW DKKRKKYVNT QGLDNKKYII
     GESGQKIPAS FRSGKFQDWS KARKIAPLKV GARESTIPSN LLADPTSPSE RTVGGKFKHK
     TQKAPKLPDK HRDDYAFQKK KVEAALERGV RVKGYNGPGM KQEIKSVDEI RKLREIKEKK
     RSKNARPTKR RKH