ID   MAK5_AJECN              Reviewed;         772 AA.
AC   A6R9U4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=ATP-dependent RNA helicase MAK5;
DE            EC=3.6.4.13;
GN   Name=MAK5; ORFNames=HCAG_05732;
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. DDX24/MAK5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476661; EDN09929.1; -; Genomic_DNA.
DR   RefSeq; XP_001538127.1; XM_001538077.1.
DR   AlphaFoldDB; A6R9U4; -.
DR   SMR; A6R9U4; -.
DR   STRING; 339724.A6R9U4; -.
DR   EnsemblFungi; EDN09929; EDN09929; HCAG_05732.
DR   GeneID; 5444605; -.
DR   KEGG; aje:HCAG_05732; -.
DR   VEuPathDB; FungiDB:HCAG_05732; -.
DR   HOGENOM; CLU_003041_13_0_1; -.
DR   OMA; HYHVPRT; -.
DR   OrthoDB; 973872at2759; -.
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; 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..772
FT                   /note="ATP-dependent RNA helicase MAK5"
FT                   /id="PRO_0000310209"
FT   DOMAIN          218..428
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          480..638
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           187..215
FT                   /note="Q motif"
FT   MOTIF           355..358
FT                   /note="DEAD box"
FT   COMPBIAS        101..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   772 AA;  85018 MW;  A3250F3D3280A706 CRC64;
     MAKKRARVAQ DLSHKSKKRQ RVEATGDDGE IVGIDQLDWK EVALPDRLED AEGFFGLEEI
     DGVDLVRPIG NGEIKFKAAR NRVKKNVANS ISSNTEHEAG EWSGISDDEE PADDRVHSSK
     GKQTNVDKIE TKEDKEKKSK KQSKKDLKLI DAEIQRKKKP APKHDIQSGI SFEALEEEVD
     GDEVDVSGWD PLGISAEIQT SLSKLRFAKP TPIQTACIPL IASGHDVVGK ASTGSGKTLA
     FGIPILEYYL KNRREEPVQH NDAELSSKYP IALILSPTRE LAHQLSKHIT ALCTNAPNIN
     ARIALLTGGL SVQKQQRVLA NADIVIGTPG RLWDVISTGH GLLRKFQNIK FLVIDEADRL
     LSEGHFKEVE EILTALDRKE IHHKVTADSE SEDDASRESP RQTLVFSATF HKGLQQKLAG
     KGRYFDGDLL DDKQSMEYLL KKLNFREDRP KFIDVNPVAQ MAENLKEGLV ECPAMEKDLY
     LYTLMLYHPQ HRTLVFTNSI SAVRRLTAFL QNLNLPALAL HSSMAQKARL RSVERFSSPT
     ADPSSILVAT DVAARGLDIK GIDLIIHYHV PRTADTYVHR SGRTARASAS GKSILLCAPE
     EIVGVARLAA KVHASSTASS SSSSSVTKRL PLHSVDLDRR VIARVRPRVA LAKKITNHAL
     AKEKLSSEND WLRSAADDLG VDYDSEEFAE QAKGKGRGRG RGGGREAREK AAGSMTKAEV
     ATLKAQLREL LGKRINMGVS ERYLTAGRVD IEALLAVGGN KTFLGQVGEL DF