DRS1_DEBHA
ID DRS1_DEBHA Reviewed; 771 AA.
AC Q6BTL5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; OrderedLocusNames=DEHA2C17534g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG86536.1; -; Genomic_DNA.
DR RefSeq; XP_458454.1; XM_458454.1.
DR AlphaFoldDB; Q6BTL5; -.
DR SMR; Q6BTL5; -.
DR STRING; 4959.XP_458454.1; -.
DR PRIDE; Q6BTL5; -.
DR EnsemblFungi; CAG86536; CAG86536; DEHA2C17534g.
DR GeneID; 2900616; -.
DR KEGG; dha:DEHA2C17534g; -.
DR VEuPathDB; FungiDB:DEHA2C17534g; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_2_1; -.
DR InParanoid; Q6BTL5; -.
DR OMA; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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; 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..771
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000232245"
FT DOMAIN 289..465
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 476..643
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..84
FT /evidence="ECO:0000255"
FT MOTIF 258..286
FT /note="Q motif"
FT MOTIF 412..415
FT /note="DEAD box"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 771 AA; 86855 MW; E633565002D5A1EC CRC64;
MAKKSNKSNK LSTLQKPSQK DFILTIDSDS EGENEIPDLE EESEVDQELK EEEKPKPKPK
PKSKKNKKNK DINNDQEKTE EQEEINPNFT FSLDGFETST AFDGWDFKVE SNGDVTKKPI
SKDVDLDGIL RRKGGLANLA GSDVKVDEKN DEVESEEVEE VEEDDEDEEN EQEGDDDDDE
LALDGFGMSA TEASANADDD QDEQEPEDDD EGVEADMDEE YPGSDQEDEK PVEDTAEDMA
EFYADEEEAT TAKKQLHTTF QSLQLSRPVL KGLSQLGYTK PSPIQSACIP IALLGKDIVA
GAVTGSGKTA AYMIPIIERL LYKPAKISST RVIVLAPTRE LAIQVCDVGK KIGQFVNNLN
FGLAVGGLNL RQQEQQLKTR PDIVIATPGR LIDHIRNSPS FSIDSLEVLV IDEADRMLDE
GFQAELTEIL SLIPRHKRQT LLYSATMNTK IQDLIQLSLQ KPVRVMIDPP KSAAIKLVQE
FVRIRKRDHL KPALLFQLIK SVDPSQQNRI VVFVARKESA HKLRIILGLL GMRVSELHGS
LTQEQRLASV NDFKNLTVPV LICTDLAARG LDIPKIEIVI NYDMPKTHEI YLHRVGRTAR
AGREGKSITF VGESTQDRAI VKDAIKSISE EQARNSKQGK AVSRNVDWKE VEELNKIVES
KATVIEEVLD EEKQAKEMLH AEMELSKATN MIKHEKEIQS RPRRTWFESE KDKKHQTEVM
QQLTKHGKKV NSHKRKAIEV KKENSSRSYK KTKQDRMSVQ KKPKSNGKNK K
