ID   DRS1_ASPOR              Reviewed;         820 AA.
AC   Q2UQI6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=ATP-dependent RNA helicase drs1;
DE            EC=3.6.4.13;
GN   Name=drs1; ORFNames=AO090005001231;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE56179.1; -; Genomic_DNA.
DR   RefSeq; XP_001818181.2; XM_001818129.2.
DR   AlphaFoldDB; Q2UQI6; -.
DR   SMR; Q2UQI6; -.
DR   STRING; 510516.Q2UQI6; -.
DR   EnsemblFungi; BAE56179; BAE56179; AO090005001231.
DR   VEuPathDB; FungiDB:AO090005001231; -.
DR   Proteomes; UP000006564; Chromosome 1.
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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..820
FT                   /note="ATP-dependent RNA helicase drs1"
FT                   /id="PRO_0000232241"
FT   DOMAIN          333..507
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          537..714
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          681..729
FT                   /evidence="ECO:0000255"
FT   MOTIF           302..330
FT                   /note="Q motif"
FT   MOTIF           455..458
FT                   /note="DEAD box"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..246
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         346..353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   820 AA;  90924 MW;  FBE29D83381BE6F7 CRC64;
     MAPPKKRTAP KDDDFVLTLS DDENDVFSGI NEDGDDHLDE ETAKSTTKKR KRDTAETTQS
     KNKKQKQQKQ SKNGKQQKKV EEAASEPEEG SEEEEDAGED DGALNSDFEF DVGAAAQKDV
     VEGFDGWGLD ETKDGAKKNG DKQGVDIDEI ISRRQAKKEA QLKKKPKKQE VESEDEGSGN
     EDDASDGGMS VDFQDDELMA EDGFGMGADG EDESGQSDAQ ESGSEDEHAG SDSEDSDDDD
     DDAASDNDSV ATPVQHPDDV ASDNDGSDIE SEVDAEEEAK RKAFFAPEEQ TSEQSAAELS
     KKSFQEFNLS RPILRGLAAV NFTNPTPIQR KTIPVALLGK DIVGSAVTGS GKTAAFVVPI
     LERLLFRPRK VPTSRVAILM PTRELAVQCY NVATKLATYT DITFCQLVGG FSLREQENIL
     KKRPDVIIAT PGRFIDHMRN SASFTVDTLE ILVLDEADRM LEDGFADELN EILTTIPKSR
     QTMLFSATMT DSVDKLIRVG LNRPVRLMVD SKKNTSMNLI QEFVRLRPGR EDKRLGYLLH
     LCKEVYTGRV IVFFRQKKEA HRVRIAFGLL GLKAAELHGS MSQEQRIRSV ENFREGKVSF
     LLATDLAARG LDIKGVETVI NYEAPQSHEI YLHRVGRTAR AGRSGRACTI AAEPDRKVVK
     AAVKASKAQG AKVASRVVDP AVADRWAQKA KDLEEEINAV LEEEKIEKQL AQAEMQVTRS
     ENMIKHEAEI MSRPKRTWFA SEREKILSKK AGAAELNGLD SVKSKKEKVR LSNKDKKRLD
     DSRQRNEGNI GWKKGKVDRE SQKQGKIQKG KKENKKKGKK