ID   DRS1_ASPTN              Reviewed;         821 AA.
AC   Q0CZN5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=ATP-dependent RNA helicase drs1;
DE            EC=3.6.4.13;
GN   Name=drs1; ORFNames=ATEG_00849;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476594; EAU39495.1; -; Genomic_DNA.
DR   RefSeq; XP_001210935.1; XM_001210935.1.
DR   AlphaFoldDB; Q0CZN5; -.
DR   SMR; Q0CZN5; -.
DR   STRING; 341663.Q0CZN5; -.
DR   PRIDE; Q0CZN5; -.
DR   EnsemblFungi; EAU39495; EAU39495; ATEG_00849.
DR   GeneID; 4355610; -.
DR   VEuPathDB; FungiDB:ATEG_00849; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   HOGENOM; CLU_003041_3_1_1; -.
DR   OMA; AAHTDIR; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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; 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.
FT   CHAIN           1..821
FT                   /note="ATP-dependent RNA helicase drs1"
FT                   /id="PRO_0000282491"
FT   DOMAIN          335..509
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          536..683
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           304..332
FT                   /note="Q motif"
FT   MOTIF           457..460
FT                   /note="DEAD box"
FT   COMPBIAS        21..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..194
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..250
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   821 AA;  90665 MW;  20B0460670BFC8F3 CRC64;
     MAPKQKDDDF VLTLSDDEND AFNNFDVDGD DGDDGDELAS SGTKKRKRDT AETTQNTSKK
     QKQQKPVKNG LKKNKKGQAE TPAEEEQEEP QEEEDAGEDD GALDSDFEFD VGGVANTVVE
     GFDGWGMGNA EDEGAAKKGD KKAVDIDDII SRRQAKKEAA EAKKKKKQSE AQDNESWDGV
     AEDEDAESDG GMSVDFQDDE LLAADGFGMG ADGEDESDNE EAQDESGSDN DSDDDEEKDS
     EDDDDEAASD NDSVATPVGH PEDEASDNDS DAESEIDAEE QEKRKAFFAP EEEKTKEQAD
     GAQRSFQEFN LSRPILRGLA AVNFTNPTPI QRKTIPVALL GKDIVGSAVT GSGKTAAFVV
     PILERLLFRP RKVPTSRVAI LMPTRELAVQ CYNVATKLAT YTDITFCQLV GGFSLREQEN
     ILKKRPDVII ATPGRFIDHM RNSASFTVDT LEILVLDEAD RMLEDGFADE LNEILTTIPK
     SRQTMLFSAT MTDTVDKLIR VGLNRPVRLM VDSKKNTSLT LVQEFVRLRP GREDKRLGYL
     LYLCKEIYTG RVIVFFRQKR EAHRVRIVFG LLGLKAAELH GSMSQEQRIK SVENFRDGKV
     AFLLATDLAS RGLDIKGVET VINYEAPQSH EIYLHRVGRT ARAGRSGRAC TIAAEPDRKV
     VKAAVKASKA QGAKVASRVV DPAVADQWAK KAADLEEEIN EVLEEEKTEK QLAQAEMQVT
     KGENLIKHEA EIMSRPKRTW FESEKDKRAA RKLGAAQLNG PDAGLSKKEK VKLSNKDKKR
     LDDARQRLEG KAGWKKGKAE REAPKPAKGK GKGKDKKKGK N