DRS1_LODEL
ID DRS1_LODEL Reviewed; 686 AA.
AC A5DY34;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; ORFNames=LELG_02271;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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; CH981525; EDK44092.1; -; Genomic_DNA.
DR RefSeq; XP_001527442.1; XM_001527392.1.
DR AlphaFoldDB; A5DY34; -.
DR SMR; A5DY34; -.
DR STRING; 379508.A5DY34; -.
DR PRIDE; A5DY34; -.
DR EnsemblFungi; EDK44092; EDK44092; LELG_02271.
DR GeneID; 5234027; -.
DR KEGG; lel:LELG_02271; -.
DR VEuPathDB; FungiDB:LELG_02271; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_2_1; -.
DR InParanoid; A5DY34; -.
DR OMA; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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:0042254; P:ribosome biogenesis; 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; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..686
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000294640"
FT DOMAIN 227..402
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 414..581
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 17..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 586..666
FT /evidence="ECO:0000255"
FT MOTIF 196..224
FT /note="Q motif"
FT MOTIF 349..352
FT /note="DEAD box"
FT COMPBIAS 94..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..686
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 686 AA; 77717 MW; 2AC3D2FEAFBCB600 CRC64;
MAKNEDLILT IDSDAEYDNI SESSEEEAEE AVSVKSKKKN NNNNNNKKSK AGKHGKANLE
EAEAEEDDDE ARGEMNLDFQ FSLGDDLNEI KDWEVEEPAK DIDLNEIIKK KRESKKDGNG
DDEEDDGDED EDASESEEDD EKEELKAAGK NGQAGDDDED ENEDEDEEEE VDTKEDLDNF
YESQETNTSA SALKSKTFQE LQLSRPILKS LQQLGFTVPT PVQASTIPIA LLGKDIVASA
QTGSGKTAAY LIPIIERLLY VKNSTSTKAI ILTPTRELAI QVHDVGRKLG QFVSNLNFGM
AVGGLSLKQQ EQQLKTRPDI VIATPGRLID HIRNSPSFSV EDVQVLIIDE ADRMLEEGFQ
EELTEILSLI PKQKRQTLLF SATMNNTKIQ DLVQLSLNKP IKVSIDPPRT VASKLEQQFV
RIRKREELKP AVLYLLLKKL EGRTVVFTRT KVEAHKLRII LGLLGLTVAE LHGALTQEQR
LANVKAFKNN VNVLICTDLA ARGLDIRIEY VINYDMPKTY EIYTHRVGRT ARAGRKGTSI
SFVGESMQDR NIVKNAIQFN SRSVARKIDW DEVEKIQTKI KLNEGAIEEV IEEEKQAREI
MRAEMQLNKA ENLMKYEKEI KSRPKRTWFK SEVMEHLTKH GKKVNAKKRK ANEERKEEGK
ERSYKKTKAD RTKLKTKAKS SSKKRK
