ID   DBP10_AJECN             Reviewed;         900 AA.
AC   A6QUM7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=HCAG_01083;
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. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476655; EDN03219.1; -; Genomic_DNA.
DR   RefSeq; XP_001544037.1; XM_001543987.1.
DR   AlphaFoldDB; A6QUM7; -.
DR   SMR; A6QUM7; -.
DR   STRING; 339724.A6QUM7; -.
DR   PRIDE; A6QUM7; -.
DR   EnsemblFungi; EDN03219; EDN03219; HCAG_01083.
DR   GeneID; 5451394; -.
DR   KEGG; aje:HCAG_01083; -.
DR   VEuPathDB; FungiDB:HCAG_01083; -.
DR   HOGENOM; CLU_003041_5_2_1; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
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; 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..900
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000310243"
FT   DOMAIN          117..289
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          330..505
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          337..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           86..114
FT                   /note="Q motif"
FT   MOTIF           237..240
FT                   /note="DEAD box"
FT   COMPBIAS        337..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..760
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..853
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..900
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   900 AA;  99968 MW;  54AC04551CEA168A CRC64;
     MPHRDVSPAA SENEFDISNL LFKGQDDLSD LERPSKKRKP QETLILDVMG DGDDGADGDE
     EFIAAQQTAA NRKASNLRGR TVKKGGGFQS LGLNAALLKA ITRKGFSVPT PIQRKTIPLV
     LDDQDVVGMA RTGSGKTAAF VIPMIEKLKS HSAKFGSRAL ILSPSRELAL QTLKVVKELG
     RGTDLKSVLL VGGDSLEEQF EYMASNPDII IATPGRFLHL KVEMSLDLSS IRYVVFDEAD
     RLFEMGFATQ LTEILHGLPS SRQTLLFSAT LPKSLVEFAR AGLQEPILIR LDAESKISPD
     LQNAFFTVKS SEKEGALLHV LHEVIKIPTG ETEALKRAKE EVKHSKKRKR SEVTSNSHKE
     SPTEHSTIIF TATKHHVDYL TSILRTSGFA VSYAYGSLDQ TARKIEVQNF RDGITHILVV
     TDVAARGIDI PILSNVINYD FPSQPKIFVH RVGRTARAGK TGWSYSLIRE SDTPYLLDLQ
     LFLGRPLILG RGSGQQLNYA ENVVVGSLPR DKVARYTEWM TKLLDEDVDI ELQREVAIKG
     EKLYMRTRNS ASGESAKRAK AVVESAEWMM VHPLFNDESS RLEEQREKML ARVGGYKPQE
     TIFEISGRRG ANHHPPDDSD DANELRDFDG ENDNAIAADN MSLASDSELE VTFSYPQSGK
     SNSKKDTNHP NLRESFHNPE YFMSYTPASN SLAEDRAYGV HSGSNTNFVE SSRIATMDLA
     GDESTSRGFG EPRSIMRWDK RQKKYVSRRN DEDGSKGGKS DLLVRGESGV KIAASFRSGR
     FDAWKKGKRI GRMPRVGEAE APGLGSGMPG GKKYRHRKEQ APKTPDKFRG DYEKKKKKLE
     AAKQRETEKA FDPSSGAKKA AVTSRGKSEL KTVEDIRKAR KVKELRKQKN ARPSKKGKGR