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 27-MAR-2024, entry version 74.
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.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476661; EDN09929.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R9U4; -.
DR SMR; A6R9U4; -.
DR STRING; 339724.A6R9U4; -.
DR VEuPathDB; FungiDB:HCAG_05732; -.
DR HOGENOM; CLU_003041_13_0_1; -.
DR OMA; QMIQKAR; -.
DR OrthoDB; 56712at2759; -.
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 CDD; cd17946; DEADc_DDX24; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR24031:SF91; ATP-DEPENDENT RNA HELICASE DDX24; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
