ID   DBP7_CRYNB              Reviewed;         948 AA.
AC   P0CQ95; Q55KZ7; Q5KAI2;
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 DBP7;
DE            EC=3.6.4.13;
GN   Name=DBP7; OrderedLocusNames=CNBJ1870;
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. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAEY01000049; EAL18545.1; -; Genomic_DNA.
DR   RefSeq; XP_773192.1; XM_768099.1.
DR   AlphaFoldDB; P0CQ95; -.
DR   SMR; P0CQ95; -.
DR   PRIDE; P0CQ95; -.
DR   EnsemblFungi; AAW45820; AAW45820; CNJ01590.
DR   EnsemblFungi; EAL18545; EAL18545; CNBJ1870.
DR   GeneID; 4938530; -.
DR   KEGG; cnb:CNBJ1870; -.
DR   VEuPathDB; FungiDB:CNBJ1870; -.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   Proteomes; UP000001435; Chromosome 10.
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; IPR025313; DUF4217.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..948
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000410258"
FT   DOMAIN          250..476
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          597..757
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          43..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           200..229
FT                   /note="Q motif"
FT   MOTIF           397..400
FT                   /note="DEAD box"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..607
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..900
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         263..270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   948 AA;  102839 MW;  A293CD6322EC7B6A CRC64;
     MADDIELNFA VPASGLVRQV APKKGGRWTD RVRAKREARD AFKSMKANHL TVQNPSMPTV
     SASELVPKPA VIKPAPTSAS VSRHPQPKSQ VVAPPRFTNA TAGPSRPAPS PQAASSNVPK
     SASIPAPATI KHRTSLPTNA FERPPLPPQA GPSRPHPAEK LKTPQFISSL FTSAPLPGVK
     SSVAPEISTG APSNAPVDTT TFQGLGLNKL LINHLKGKMG VEKPTGIQRN CLPYMLSSPL
     NPDKKAGDEG PKEEPLRDVL IQAQTGSGKT LSYLLPIVQT LLPLSRLSYI DRSIGTLAII
     LAPTRELAQQ ISKVLEQLLH MSFAASKEGS DDEDEDDRPF TRWLVSGLLT GGSTRTHEKA
     KLRKGVPILV STPGRLLDHL QNTMSFQCAK TMFLVLDEAD RLMDLGFEET IQGIIKALEG
     RRRNEINIEK EMDKEGGGTM RWPFWDRGRL NVLCSATVDA KVERLAGAAL RDPVLFRSEK
     DEAEAKKKAE GKDDAVIKAL NEAQAIVIPQ ESEEKFTPPS QLSQKYVVLP TKLRLVALVA
     LLRSLISSVA KGISVSNGTK VIVFLSSTDA VDFHWKLLGG VQMGQQGQQA DGEKEEDEEE
     EGESVEERES DGESKAKKSK RKAKSKSTDD IVSLASPLFP NTTLHRLHGS LPLRTRLASL
     KAFATSSSQP SVLFATSVAS RGLDLPLVRA VVQYDLPTEG GANEYVHRVG RTARAGKGGE
     AWAFVSPSEE GWVKWIEGKM GAAEGKSGVN LGQVGVEDVL RKGFGGKSYE YEARATDVQL
     SFENWVLASE QNAALARKAF ASFVRAYSTH PLEEKQFFHT KLLHLGHLAK SFALREAPAQ
     LASALSAGKS KRPKSKAASS ATHPGKRKRD EDEDEMEERG GKELTARNET ERRMYEAVRK
     QGRTIKSGGK LGEFSGKGQN KGQKAAATGG EFHIVNTGEL ERLVARRK