ID   DRS1_ASPNC              Reviewed;         824 AA.
AC   A2QAX7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=ATP-dependent RNA helicase drs1;
DE            EC=3.6.4.13;
GN   Name=drs1; ORFNames=An01g13150;
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 ribosome assembly.
CC       {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   -!- SUBUNIT: Associates with pre-ribosomal particles. {ECO:0000250}.
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. DDX27/DRS1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM269986; CAK37361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QAX7; -.
DR   SMR; A2QAX7; -.
DR   PaxDb; A2QAX7; -.
DR   EnsemblFungi; CAK37361; CAK37361; An01g13150.
DR   HOGENOM; CLU_003041_3_2_1; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
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; 2.
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.
FT   CHAIN           1..824
FT                   /note="ATP-dependent RNA helicase drs1"
FT                   /id="PRO_0000282490"
FT   DOMAIN          340..514
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          541..685
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           309..337
FT                   /note="Q motif"
FT   MOTIF           462..465
FT                   /note="DEAD box"
FT   COMPBIAS        15..37
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..112
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..202
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..255
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         353..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   824 AA;  91785 MW;  A4E349E095E8321D CRC64;
     MAGTKKRANA DDDFVLTLSD DENDTLNQLE EEGEGDDGAL ATGSKTKKRK RDDAAAAQQE
     KGKNKKVKKQ EQQQQQAQQK KKKGKNAPVQ EEEDEDEEEE EDQGEDDGAL NSDFEFDVGG
     AANEVRDFDG WEVNGNEEGK GGDKKAVDID DIISRRQAKK EAELIRKQKK KKQKQEEEFS
     ELEDDDEEDG GMEVDFGDDE LLAEDGFGMG VDGEEESEKS DAEDEEKEEG SDEEAEGSDE
     DEQMDEDDDD AASDDDSVAT PVMHPDDIAS DRDSDEESQV DAEEEEKRKA FFAPEEEKTS
     ESAMADAKRS FQEFNLSRPI LRGLAGVNFS NPTPIQRKTI PVALLGKDIV GSAVTGSGKT
     AAFVVPILER LLFRPRKVPT SRVAILMPTR ELAVQCYNVA TKLATYTDIT FCQLVGGFSL
     REQENILKKR PDVIIATPGR FIDHMRNSAS FTVDTLEILV LDEADRMLED GFADELNEIL
     TTIPKSRQTM LFSATMTDTV DKLIRVGLNR PVRLMVDAKK NTAVTLVQEF VRLRPGREDK
     RLGYLLYLCK EIYTGRVIVF FRQKKEAHRV RIIFGLLGLK AAELHGSMSQ EQSVENFREG
     KAAFLLATDL ASRGLDIKGV ETVINYEAPQ SHEIYLHRVG RTARAGRSGR ACTIAAEPDR
     KVVKAAVKAG KSQGAKIASR VIEPAVADSW AAKAEELADE VEEVLSEEKL EKQLAQAEMQ
     VTKGENLIKH EAEIKSRPKR TWFETERDKK AARKLGAAEL NGPDAGMSKK EKQKLSNKDK
     KRLDDSRQRQ EAGAGWKKGR ATRESMKNGQ LPKAKKDNKK KGKK