MAK5_ASPNC
ID MAK5_ASPNC Reviewed; 766 AA.
AC A2QWW0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ATP-dependent RNA helicase mak5;
DE EC=3.6.4.13;
GN Name=mak5; ORFNames=An11g06650;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270241; CAK96962.1; -; Genomic_DNA.
DR RefSeq; XP_001394643.1; XM_001394606.1.
DR AlphaFoldDB; A2QWW0; -.
DR SMR; A2QWW0; -.
DR PaxDb; A2QWW0; -.
DR PRIDE; A2QWW0; -.
DR EnsemblFungi; CAK96962; CAK96962; An11g06650.
DR GeneID; 4984889; -.
DR KEGG; ang:ANI_1_876094; -.
DR VEuPathDB; FungiDB:An11g06650; -.
DR HOGENOM; CLU_003041_13_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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..766
FT /note="ATP-dependent RNA helicase mak5"
FT /id="PRO_0000282485"
FT DOMAIN 223..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 485..635
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..220
FT /note="Q motif"
FT MOTIF 360..363
FT /note="DEAD box"
FT COMPBIAS 10..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 766 AA; 84685 MW; F71D94FB0CBBACCB CRC64;
MGQKRQRGSK SADLQAKKRK KDVSAVEDGE DALVTVNDLN WKEVALPDRL EDAGGFFGLE
EIDGVEVIKG GSEGLRFKAA HGKPKKSILK KKAPEEEEPK FDDDEWSGFS DNEVTEKKDT
APKEDQKDEQ EADKPTAEEK KKAKKDRQAE QKKAKKEAKQ KTTPNQEDKS IKPGLSFAAL
QDEEDDDGVD VSAWESLGLS PEILTSLSKM KFTTPTLVQK SCIPQILDGH DVIGKASTGS
GKTLAFGIPI LEHYLEKRRQ DLRAGKEEKK KDTAPIALIM SPTRELAHQL AKHIGELALH
APGSNARIAL LTGGLSVQKQ QRVLAGADIV IGTPGRVWEV LSSGQGLIRK MSEIKFLVID
EADRLLSEGH FKEAEEILGA LDRVEEGNFG GEESEDEEKE DARSERQTLV FSATFHRDLQ
QKLAGKARWT GGDIMSNKES MEYLLQKLKF REEKPKFIDV NPVSQMAEGL KEGIVECGAM
EKDLYLYTLL LYNPKHRTLV FTNSISAVRR LTQLLQNLGL PALALHSSMA QKARLRSVER
FSSPTSDPSS ILVATDVAAR GLDIKGIDFV IHYHAPRAAD TYVHRSGRTA RAGASGKSVI
ICAPEEMVGV VRLAAKVHAN MANGKKLPLE SLELDRRVVL RVRQRVDLAA KITDSNIAKE
KISAEDNWLQ KAAEDLGVEY DSEEFESAQG RGRGRGRGRQ ERQRKAGEVT KNELAAMRAE
LKHLLSQRVN VGVSERYLTS GRVDIEALLR GEGNNSFLGQ VDPLDF
