ID   DBP9_CRYNB              Reviewed;         627 AA.
AC   P0CR11; Q55I26; Q5K7L2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; OrderedLocusNames=CNBM1920;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAEY01000064; EAL17387.1; -; Genomic_DNA.
DR   RefSeq; XP_772034.1; XM_766941.1.
DR   AlphaFoldDB; P0CR11; -.
DR   SMR; P0CR11; -.
DR   EnsemblFungi; AAW46985; AAW46985; CNM02050.
DR   EnsemblFungi; EAL17387; EAL17387; CNBM1920.
DR   GeneID; 4939552; -.
DR   KEGG; cnb:CNBM1920; -.
DR   VEuPathDB; FungiDB:CNBM1920; -.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   Proteomes; UP000001435; Chromosome 13.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..627
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000410266"
FT   DOMAIN          52..238
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          249..487
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          337..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           40..48
FT                   /note="Q motif"
FT   MOTIF           181..184
FT                   /note="DEAD box"
FT   COMPBIAS        337..366
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..614
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   627 AA;  68915 MW;  576E9E4ADA4BB300 CRC64;
     MLSKSNQPSD ALLDADFSFS QPPFSTLIDS RVLVALADQK FAHPTLVQAK AIPLLLEGKD
     VLARARTGSG KTAAYIVPAV QKILEAKADL SPASAEYQAT RAIILVPTKE LALQVSSFTK
     NVTKYCDGLV QCVDVAAGGA SIQRVLLNDK PDIVISTPTK LLSLLQSKSL SLSQLSFLAI
     DEADLLLSYG FKDDLTRIMD PTSGWIPKLG VQGCLMSATL SDDVEGIKGL VLRNPAILTL
     SEPASASSLL SQHYTHTSER DKFLLIYVLL KLKLIRGKSI IFVNDVERGY RVKLFLEQFG
     VKCCVVNSEL PLASRYHVVE EFNRGVYDVV VATDEGAGAD AEEEEDVKQE ESESEGEEDE
     DDDKEAEDKE KEAKEEAKPA PGPSKRRATS PPSKPNKRAR RADPTSSLAR GIDFTSASSV
     INFDLPLTST SYMHRVGRTA RAGQSGLALS FVVPRENWGK DKAVSIKSAE KDEKVFERIK
     ERVKKESDSE IKEWDWKGRK GEIEGFRYRM EDALKAVTGK RVAEARREEV RRELLNSEKL
     KSHFAANPLD LSYLRHDAPL HPARQQTHLK HVPNYLMPKI AALPTGGDVT DHAGVGFSRR
     GRGGHRGRGG RGSKSGRGKK VDPLKFK