ID   MAK5_COCIM              Reviewed;         783 AA.
AC   Q1E7Y4; J3KJ71;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=ATP-dependent RNA helicase MAK5;
DE            EC=3.6.4.13;
GN   Name=MAK5; ORFNames=CIMG_01329;
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. DDX24/MAK5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GG704911; EAS35975.3; -; Genomic_DNA.
DR   RefSeq; XP_001247558.1; XM_001247557.2.
DR   AlphaFoldDB; Q1E7Y4; -.
DR   SMR; Q1E7Y4; -.
DR   STRING; 246410.Q1E7Y4; -.
DR   PRIDE; Q1E7Y4; -.
DR   EnsemblFungi; EAS35975; EAS35975; CIMG_01329.
DR   GeneID; 4568065; -.
DR   KEGG; cim:CIMG_01329; -.
DR   VEuPathDB; FungiDB:CIMG_01329; -.
DR   InParanoid; Q1E7Y4; -.
DR   OMA; HYHVPRT; -.
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; 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   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.
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..783
FT                   /note="ATP-dependent RNA helicase MAK5"
FT                   /id="PRO_0000256020"
FT   DOMAIN          221..438
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          490..648
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           190..218
FT                   /note="Q motif"
FT   MOTIF           359..362
FT                   /note="DEAD box"
FT   COMPBIAS        1..22
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   783 AA;  86750 MW;  C230B82DAF7C3BFE CRC64;
     MAQKRSHNHK DHTAKAIKRR KFNAATAKSS DDAAHDIVSV DQLDWKTVTL PDRLDDAEGF
     YGLEEIEGVD ILRPSGGGEI KFKASKSKIK GILKNSTDKS GQPAEDWEEW SGFGDDSEDG
     DGTTLEAEKK AENHGKVNDR RTKTNNSNKE KESNKLPKDR GPRIKTDNGI KTGVSFAALQ
     DEVEEDVDVS AWDSLDLSAE LQTSLGRLKF SSPTPIQSAC IPAVLQGHDV IGKASTGSGK
     TLAFGIPIVE YFLGKYRGGR APTASEERES TKEPMALILS PTRELAHQLN KHLTDLVNHA
     PNTQVRIATV TGGLSIYKQQ RLLADADIII ATPGRLWEVV GSMTGFLSKL KKIRFLVIDE
     ADRLLSEGHF KEVEEILNAI DKVEITEEAY GERSEREPEP EPDEEKKAEP RQTLVFSATF
     HKGLQQKLSG KIRYRNDDLL DKKESMEYLL RKLNFREERP KFIDVNPISQ MAQNLKEGLV
     QCAPMDKDLL LYTLLLYHPK HRTLVFTNSI SAVRRLTQLL QNLNLPTFAL HSSMAQKARL
     RSVERFSSLS SDPSSILVAT DVAARGLDIK GIDLIVHYHI PRTADTYVHR SGRTARASAS
     GKSILICAPE ETTGVARLVA KIHSNKKDSS ATESKMEKKV PLQSVDLDRR IIDRLRPRVT
     LAKKITESIL AKEKLSSEDD WLRSAAEDLG VDYDSDEFAE QQSKGKGKGR GRGGGRQARE
     QKAASLSKAE LAGLKAQLRE LVSKKVNVGI SEKYLTAGRV DVDALLRGEG NDAFLGHVEK
     LSF