DRS1_YARLI
ID DRS1_YARLI Reviewed; 753 AA.
AC Q6CEB8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; OrderedLocusNames=YALI0B16896g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83247.1; -; Genomic_DNA.
DR RefSeq; XP_500994.1; XM_500994.1.
DR AlphaFoldDB; Q6CEB8; -.
DR SMR; Q6CEB8; -.
DR STRING; 4952.CAG83247; -.
DR EnsemblFungi; CAG83247; CAG83247; YALI0_B16896g.
DR GeneID; 2907091; -.
DR KEGG; yli:YALI0B16896g; -.
DR VEuPathDB; FungiDB:YALI0_B16896g; -.
DR HOGENOM; CLU_003041_3_1_1; -.
DR InParanoid; Q6CEB8; -.
DR OMA; AAHTDIR; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; 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..753
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000232249"
FT DOMAIN 283..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 487..636
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 649..729
FT /evidence="ECO:0000255"
FT MOTIF 252..280
FT /note="Q motif"
FT MOTIF 406..409
FT /note="DEAD box"
FT COMPBIAS 35..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 753 AA; 84204 MW; C3C22A26A1E9B989 CRC64;
MVKGKVTKPV KKATKSKQSA AMISKVKDDF VMTLDSDGED LEEESADEKE EVEEKPVKLT
KKQKKQKLSE ADEELLEREK QAAKAGINPD FQFSLDGFAA TSEGLDGWNF EVSKDDNKVQ
KREVDLDSII KRKGGLLDED EDEDEAETDV KMEENEDDLA IDGFGGGVQP GKDMDEPEDE
DEENKEEVEN EEEEDSDGSD SEAEECMHPD DLVLDDHKGP AIDEGPQDTA EEMAAFYAPE
EENNDKTESV HKTFQTLNLS RPVMKGISAL GYQAPTPIQS RTIPIALMGK DLVAGAVTGS
GKTAAYIIPV LERLLYKSSK VAATKVVVLT PTRELSIQVA DVGKKLAQYV SGVRFGLAVG
GLNLRVQEQE LKTRPEVVIA TPGRFIDHVR NSPSFNVDDV EILVIDEADR MLEEGFQQEL
TEILTLLPKK RQTLLFSATM NSSISSLIQL SLSRPVRVMI NPPKQAASGL VQEFVRIRKR
DHLKPALLAS ILKKMDKEQR TIIFVARKET AHRLRIMLGL LGVRIGELHG ALSQEQRLQS
ITAFKKLEVP ILVCTDLASR GLDIPKIECV VNYDMPQTHA VYLHRVGRTA RAGREGRSIT
LVGEAAADRA IVREAIKSVS ESKQGKAVGR NVDWPEVEKL YSKIEEKGDI VNEILAEEKE
EKAMLQAEME VRKGENLLKY EKEIASRPRR TWFQNAQEKK ADETSDKRNL LASNKDKMKK
KKDNEEVRMY KKTKTDRKEA SKRGKPKGKG KRK
