ID   DBP4_CRYNJ              Reviewed;         859 AA.
AC   P0CQ82; Q55YW1; Q5KN79;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; OrderedLocusNames=CNA07420;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
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-dependent RNA helicase required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2 (By similarity).
CC       {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   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes (By similarity). {ECO:0000250}.
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. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE017341; AAW41239.1; -; Genomic_DNA.
DR   RefSeq; XP_567058.1; XM_567058.1.
DR   AlphaFoldDB; P0CQ82; -.
DR   SMR; P0CQ82; -.
DR   STRING; 5207.AAW41239; -.
DR   PaxDb; P0CQ82; -.
DR   eggNOG; KOG0343; Eukaryota.
DR   HOGENOM; CLU_003041_26_1_1; -.
DR   InParanoid; P0CQ82; -.
DR   OMA; YDKMFER; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000002149; Chromosome 1.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; 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:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; 1.
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..859
FT                   /note="ATP-dependent RNA helicase DBP4"
FT                   /id="PRO_0000256002"
FT   DOMAIN          91..274
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          288..463
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           60..88
FT                   /note="Q motif"
FT   MOTIF           213..216
FT                   /note="DEAD box"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..596
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         104..111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   859 AA;  95611 MW;  BBC3D758ACD30A12 CRC64;
     MALGDKNQGS SKSQAKQKGT KGKNAQPRLK SNQLKRLKIN EELKELQSRV DNFVPPSEIT
     LFSELPMSSK TQKGLKSSHF LNPTPIQSLA IPPALQARDI LGSAKTGSGK TLAFLIPLLE
     RLYLEKWGPM DGLGAVVISP TRELAVQTFM QLRDIGKYHN FSAGLVIGGK PLKEEQERLG
     RMNILIATPG RLLQHLDSTV GFDSSAVKVL VLDEADRLLD LGFLPALKAI VSHFSPVQTA
     PGSRPSRQTL LFSATQSKDL AALAKLSLYE PLYISCNKPG EEGVMPANLE QYYAVVPLER
     KLDALWGFVK SHLKMKGIVF VTSGKQARRV RFIFETFRRL HPGLPLMHLH GKQKQPTRLD
     IFQRFSSSKS ALLICTDVAA RGLDFPAVDW VIQLDCPDDV DTYIHRVGRT ARYQSAGTAL
     TILCPSEEEG MKTRWGEKAI EVKRIKIKEG KMGNLKQSMQ NFAFKEPEIK YLGQRAFISY
     MKSVHIQKDK SIFKIDALPA EAFAESMGLP GAPQIKLGNQ KAAKVRGPSK EELARKAEKE
     EEEEEERAVV GSDEESEEDE SEGLGSEDEE EEIDDEAEEI DDEEESGEES GSDEETEEEK
     DASKPKAPAV RTKYDRMFER KNQSILTPHY TALIAHDADN AAGAGEADDD DDVFTLARRD
     HNLSDDEEAD TDAILGAEAL AAELKKPLIT SEDLSKRKLK AAASKKGLLK SRPGPEKVLF
     DEETGEAREF YKSGVDVEKE MSAADKRREY LEKEREIMKI QDKIDKEVAR EKKKELKRKR
     KERERELRQM EMGDEPVAYL GGDDDYASAD EGRSLSPSPA PSLEPERHAK KQRRGGVQES
     GAGDLEDEEA LALRLLQGS