ID   DBP3_COCIM              Reviewed;         515 AA.
AC   Q1DZK8; J3KDK3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=ATP-dependent RNA helicase DBP3;
DE            EC=3.6.4.13;
GN   Name=DBP3; ORFNames=CIMG_04255;
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-dependent RNA helicase required for 60S ribosomal subunit
CC       synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC       site A3, which is necessary for the normal formation of 25S and 5.8S
CC       rRNAs (By similarity). {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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GG704916; EAS33231.3; -; Genomic_DNA.
DR   RefSeq; XP_001244814.2; XM_001244813.2.
DR   AlphaFoldDB; Q1DZK8; -.
DR   SMR; Q1DZK8; -.
DR   STRING; 246410.Q1DZK8; -.
DR   PRIDE; Q1DZK8; -.
DR   EnsemblFungi; EAS33231; EAS33231; CIMG_04255.
DR   GeneID; 4565213; -.
DR   KEGG; cim:CIMG_04255; -.
DR   VEuPathDB; FungiDB:CIMG_04255; -.
DR   InParanoid; Q1DZK8; -.
DR   OMA; TQHDKAH; -.
DR   OrthoDB; 471730at2759; -.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 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..515
FT                   /note="ATP-dependent RNA helicase DBP3"
FT                   /id="PRO_0000255993"
FT   DOMAIN          130..306
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          335..484
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           100..127
FT                   /note="Q motif"
FT   MOTIF           252..255
FT                   /note="DEAD box"
FT   COMPBIAS        31..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         143..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   515 AA;  57087 MW;  2240672644D0D782 CRC64;
     MAKRPLQTEA NVERLPSELK RRKKKNSLKV TPGTVIGQNS KSRRNVPGMD DGNDKRASDS
     RYLPTPELSA LPQSTIDEYL SSNSIHIADP STDPSLRPIT SFSFLPESSN DLYLPLEKFS
     SPTPIQAVSW PLAFAGRDLI GVAETGSGKT LAFGLPCLRR VLELNNSETS CKPCALIITP
     TRELAVQIYD QLLRFSSAVD VGIACIYGGS PKDHQRREIR NASVVIATPG RLKDFQADQT
     INLSGVKYLV LDEADRMLDK GFEQDIQDIV KGIPSTQKRQ TIMFTATWPI GVRNLAASFT
     KNPVTVTIGD SSDIRANKRI KQMVEVLQPY EKDSRLLELL RRYQDGGKNN HRILVFCLYK
     KEAMRVERFI GSKGFKVAGI HGDMSQTERF RSLEAFKSGS ISLLVATDVA ARGLDIPAVK
     LVLNVTFPLT IEDYVHRIGR TGRAGAEGLA ITLFTERDKA LSGPLINVLR AADQDVPESL
     LKFGATVKKK QHESYGAFFR EMDTTKVASR IKFED