ID   DBP7_COCIM              Reviewed;         769 AA.
AC   Q1E9T9; J3KHL5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=ATP-dependent RNA helicase DBP7;
DE            EC=3.6.4.13;
GN   Name=DBP7; ORFNames=CIMG_00674;
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. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GG704911; EAS35320.3; -; Genomic_DNA.
DR   RefSeq; XP_001246903.1; XM_001246902.2.
DR   AlphaFoldDB; Q1E9T9; -.
DR   SMR; Q1E9T9; -.
DR   STRING; 246410.Q1E9T9; -.
DR   PRIDE; Q1E9T9; -.
DR   EnsemblFungi; EAS35320; EAS35320; CIMG_00674.
DR   GeneID; 4565651; -.
DR   KEGG; cim:CIMG_00674; -.
DR   VEuPathDB; FungiDB:CIMG_00674; -.
DR   InParanoid; Q1E9T9; -.
DR   OMA; AVHIKAD; -.
DR   OrthoDB; 973872at2759; -.
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; 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; 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; 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..769
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000256025"
FT   DOMAIN          188..389
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          430..622
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          38..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           155..184
FT                   /note="Q motif"
FT   MOTIF           325..328
FT                   /note="DEAD box"
FT   COMPBIAS        48..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         201..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   769 AA;  84499 MW;  6C44E7DC0BE2CD3A CRC64;
     MAEDGMLLNF SLDDSVIKPQ QRFKGGTWKD RLVAKKIAVK RQNKSRHSAE TGAVNSNNPQ
     NPNKINVPTG QRPAKRQRID GGDFKPTTKS SAGGGGVGND EQTDRKSYGD RQVISSLFTY
     NPTAKTVAST DGATHDEDTT EPAKPSNAPL VDGIDTFTSL GLSPSLATHL LTKLNLKTPT
     AIQKSSITQL LKEECDAFVQ AQTGSGKTLA YLLPIVERLM RISSHNKGKK DSEGNTVHRD
     SGLFAIVLAP TRELCKQISV VLDGLLRCAH WIVAGTVIGG EKKKSEKARL RKGLNILVAT
     PGRLADHLEN TKVLDVSNVR WLVLDEGDRL MDLGFEEEIQ GIIKKLDERR RPSKIPDLPA
     KRTTILCSAT LKMNVQRLGE ISLKEAIHIK ADPADEDDEQ KDGSKQPEFS APAQLKQSYA
     VVAAKLRLVT LTALLKRTFA RKGSVMKAII FVSCADSVDF HFEVFTRRES SEELPDADDE
     NAPSSSNVHG SIATASAFSN PSNNVILHKL HGSLPQHVRT ATLSAFAKQK DASVLICTDV
     AARGLDLPNV DFVIEYDPAF CSDDHLHRIG RTARLGRDGR ALIFLLPGNE EGYVDILKGS
     YREGSSNSVT RNEVNEILKR GFGGNSEAIS KGWEDKATDW QLDIERWALE DSTILEMARR
     AYQSHIRAYA THIAAERHMF NIKDLHLGHL AKSFALRDRP AKINVPGLRP GNEDTKKSFK
     ADRKLASGEK RKMSAREDSS STTDAAEARK KMQQKLKEHM AGASEFNIA