ID   DBP10_COCIM             Reviewed;         927 AA.
AC   Q1EB38; J3KGI4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=CIMG_00225;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704911; EAS34871.1; -; Genomic_DNA.
DR   RefSeq; XP_001246454.1; XM_001246453.2.
DR   AlphaFoldDB; Q1EB38; -.
DR   SMR; Q1EB38; -.
DR   STRING; 246410.Q1EB38; -.
DR   PRIDE; Q1EB38; -.
DR   EnsemblFungi; EAS34871; EAS34871; CIMG_00225.
DR   GeneID; 4566960; -.
DR   KEGG; cim:CIMG_00225; -.
DR   VEuPathDB; FungiDB:CIMG_00225; -.
DR   InParanoid; Q1EB38; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000001261; 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..927
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000256045"
FT   DOMAIN          112..284
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          348..502
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           81..109
FT                   /note="Q motif"
FT   MOTIF           232..235
FT                   /note="DEAD box"
FT   COMPBIAS        1..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..875
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        909..927
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         125..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   927 AA;  102549 MW;  07DBFBB16675C982 CRC64;
     MSENEFDIAK SLFQDEADSD IDTRPRKRKA PTSLNLDVMA DDNGDGDDGG SDDDAAFIAA
     HQASMNRKAS NLKGRTVKKG GGFQAMGLNA NLLKAITRKG FSVPTPIQRK TIPLVLDDQD
     VVGMARTGSG KTAAFVIPMI EKLKSHSTKV GSRGLILSPS RELALQTLKV VKELGRGTDL
     KCVLLVGGDS LEEQFGYMAG NPDIIIATPG RFLHLKVEMN LDLSSIKYVV FDEADRLFEM
     GFAAQLTEIL HGLPQSRQTL LFSATLPKSL VEFARAGLQE PTLVRLDTES KISPDLQSVF
     FTVKSAEKEG ALLHILHDVI KVPTGETEAG KHAREQAISG KSSKKRKRSE QNNPNPQESP
     TEHSTIIFVA TKHHVDYIAS LLRESGFAVS YAYGSLDQTA RKIQVSNFRT GISNILVVTD
     VAARGIDIPI LENVINYDFP SQAKIFVHRV GRTARAGRKG WSYSLVRDAD APYLLDLQLF
     LGRRLVMGRG QQESANFAED VVVGGMARES IARSCEWVSK LLDEDIDIQN QREVAMKGEK
     LYIRTRNSAS AESAKRAKDV VASDGWTMLH PLFNNEASQM EVEREKMLAR IGGYKPQETI
     FEISGRRGGK AGDDEAIDMM RKIRSTMENK RAKKQDANQP TTDAEVPASA LATTLGDDKD
     NGLGDDMDQD DVADMSMASD SELEVTFSYQ SDKSKSKKKS GDKQSSGTFQ NPEYFMSYTP
     AAHSFAEERG YGVHSGSNSN FVEASRDATM DLSRDEANRG FAEPRSIMRW DKRHKKYVSR
     RNDEDGSKGA LLVKGESGAK IAASFRSGRF DAWKKSKRLG RMPRVGETEN PGLGSTVPAR
     GQKFRHNKEQ APKAADKYRG DYEKRRKKEQ ELQKRQAETG MLQFGSKGGT KKVKSEIRSV
     DDVRKARKLK EKRREKNARP SKKGKAR