ID   DBP9_AJECN              Reviewed;         625 AA.
AC   A6R2L6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; ORFNames=HCAG_03874;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476657; EDN07343.1; -; Genomic_DNA.
DR   RefSeq; XP_001541776.1; XM_001541726.1.
DR   AlphaFoldDB; A6R2L6; -.
DR   SMR; A6R2L6; -.
DR   STRING; 339724.A6R2L6; -.
DR   EnsemblFungi; EDN07343; EDN07343; HCAG_03874.
DR   GeneID; 5448071; -.
DR   KEGG; aje:HCAG_03874; -.
DR   VEuPathDB; FungiDB:HCAG_03874; -.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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.
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..625
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000310254"
FT   DOMAIN          55..233
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          260..485
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..52
FT                   /note="Q motif"
FT   MOTIF           181..184
FT                   /note="DEAD box"
FT   COMPBIAS        339..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   625 AA;  69684 MW;  15AFD601A71DCB5B CRC64;
     MKRKLDANNV PSPEDSAGKS ITAHSFETLK LDPRLLQALT QQKFTKPTPI QAEAIPLALD
     GKDVLARAKT GSGKTAAYLL PVLQSILQQK RNTPAHKSIS ALILVPTREL AEQVHRTAIS
     FSAFSGKHVR SVNLTQKVSD AVQRSLLADL PDIVVSTPAR AVANVNSSAL SLERLTHLVI
     DEADLVLSYG YEEDMQSLAK AVPRGVQTFL MSATFTSEVD TLKGLFCRNP VVLKLEEKED
     EGAGISQFVV RRCAEDEKFL LTYVIFKLQL VKGKCIIFVG DVDRCYRLKL FLEQFGIRSC
     VLNSELPVNS RIHVVQEFNK GVYDIIIAVD DQEVLGELRK NSKKQPRKSD QCSRDSEYDG
     AQTSRNNDQY SSEDDAETQP SKRPKKSAKE KDYGISRGID FQNVACVLNF DLPTTSKSYT
     HRIGRTGRAG KTGMALSFVI PSDQFGKHKP TSIPSAKHDE AMLSKIIKRQ DKLGREVKPY
     HFDMKQVDAF RYRMSDALRA VTRVAVQEAR AREIRQELVK SEKLKRHFEE NPEELRQLRH
     DGELRAARVQ AHLKHVPDYL MPTKGRGSLS IGTGADVGFV GFKKTHENVI RKAREKNKGR
     GRGGKAGRGG KRVDPLKSFN SGGKH