ID   DRS1_KLULA              Reviewed;         748 AA.
AC   Q6CJV1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP-dependent RNA helicase DRS1;
DE            EC=3.6.4.13;
GN   Name=DRS1; OrderedLocusNames=KLLA0F15752g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382126; CAG98496.1; -; Genomic_DNA.
DR   RefSeq; XP_455788.1; XM_455788.1.
DR   AlphaFoldDB; Q6CJV1; -.
DR   SMR; Q6CJV1; -.
DR   STRING; 28985.XP_455788.1; -.
DR   PRIDE; Q6CJV1; -.
DR   EnsemblFungi; CAG98496; CAG98496; KLLA0_F15752g.
DR   GeneID; 2895875; -.
DR   KEGG; kla:KLLA0_F15752g; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   HOGENOM; CLU_003041_3_2_1; -.
DR   InParanoid; Q6CJV1; -.
DR   OMA; AAHTDIR; -.
DR   Proteomes; UP000000598; Chromosome F.
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..748
FT                   /note="ATP-dependent RNA helicase DRS1"
FT                   /id="PRO_0000232247"
FT   DOMAIN          264..439
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          468..628
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          632..667
FT                   /evidence="ECO:0000255"
FT   MOTIF           233..261
FT                   /note="Q motif"
FT   MOTIF           387..390
FT                   /note="DEAD box"
FT   COMPBIAS        53..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..154
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..188
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         277..284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   748 AA;  84048 MW;  5B24C538C40FF63F CRC64;
     MAVKKFRSFD DFVPTISDSE EDVPDLDASD DEMEKKPVKS SKTKNKSKKK AKQQQGSHLD
     EDVHEDLNPE FQFSIDSGEV TTNFAGWDFQ GDEKSDEVEK KDVDLDGIIR RKGGLIMMAA
     TGSDAEESLS EESEEEPEEG DEPGESDDED ELALDGFGMG VKRKATEENE EDEEDEEEED
     DDEDDDKKTE MSQADLGKGK DEDEDIEEDT KEEMAEFYAP EEESADAKKI VHKTFNSLSL
     SRPVLKGLGS LGYTSPSPIQ SAAIPIALLG KDIIAGAVTG SGKTAAFMIP IIERLLYKPA
     HIASTRVVVL TPTRELAIQV ADVGKNIGKF VNGLTFGLAV GGLNLRQQEQ ALKTRPDIVI
     ATPGRFIDHL RNSASFSVDS VEILVIDEAD RMLEEGFQEE LQEIMSLIPS KRQTLLFSAT
     MNSKIKQLIS LSLKKPVRIM IDPPKQAADK LTQEFIRIRK RDHLKPALLY QLIRKLDNTS
     QKRIVVFVAR KETAHKLRIV LGLLGMQVGE LHGSLTQEQR LQSVNNFKSL QVPVLICTDL
     ASRGLDIPKI EVVINFDMPK TYEIYLHRVG RTARAGREGR SVTFVGESSQ DRSIVRSAIR
     SVEENAESGK ALSRNVDWTQ VEQVNSLIGA KGDVVEEIIE EEKQEKEILR AEMELRKGEN
     MLKHKEEISA RPRRTWFQSE AEKKNSKMLQ VLAKNKKPIN SKKRKQQEAL AENPRLYKKT
     QKDRVEYQER QYSKKQAAYG KKGKKGKK