DRS1_YEAST
ID DRS1_YEAST Reviewed; 752 AA.
AC P32892; D6VXZ4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
DE AltName: Full=Deficiency of ribosomal subunits protein 1;
GN Name=DRS1; OrderedLocusNames=YLL008W; ORFNames=L1345;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1454790; DOI=10.1073/pnas.89.23.11131;
RA Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.;
RT "A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae
RT ribosome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11131-11135(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=8247005; DOI=10.1128/mcb.13.12.7901-7912.1993;
RA Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.;
RT "DRS1 to DRS7, novel genes required for ribosome assembly and function in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:7901-7912(1993).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF MET-191; ALA-260; ALA-273; PRO-288; GLU-291;
RP VAL-305; ILE-306; LEU-414; LEU-429; LEU-431; ARG-472; LEU-509; TYR-563;
RP LEU-564 AND ASP-637.
RX PubMed=11911362; DOI=10.1017/s1355838202010026;
RA Adams C.C., Jakovljevic J., Roman J., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Saccharomyces cerevisiae nucleolar protein Nop7p is necessary for
RT biogenesis of 60S ribosomal subunits.";
RL RNA 8:150-165(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP INTERACTION WITH RRP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: ATP-binding RNA helicase involved in ribosome assembly.
CC {ECO:0000269|PubMed:11911362, ECO:0000269|PubMed:1454790,
CC ECO:0000269|PubMed:8247005}.
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: Interacts with RRP1 and associates with pre-ribosomal
CC particles. {ECO:0000269|PubMed:15100437}.
CC -!- INTERACTION:
CC P32892; Q12389: DBP10; NbExp=4; IntAct=EBI-6170, EBI-5644;
CC P32892; Q04660: ERB1; NbExp=4; IntAct=EBI-6170, EBI-28098;
CC P32892; P43586: LOC1; NbExp=4; IntAct=EBI-6170, EBI-22906;
CC P32892; P37838: NOP4; NbExp=4; IntAct=EBI-6170, EBI-12122;
CC P32892; P40693: RLP7; NbExp=3; IntAct=EBI-6170, EBI-15415;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:1454790,
CC ECO:0000269|PubMed:14562095}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA34666.1; Type=Frameshift; Evidence={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; L00683; AAA34666.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X91488; CAA62783.1; -; Genomic_DNA.
DR EMBL; Z73113; CAA97452.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09310.1; -; Genomic_DNA.
DR PIR; S64750; S64750.
DR RefSeq; NP_013093.1; NM_001181828.1.
DR AlphaFoldDB; P32892; -.
DR SMR; P32892; -.
DR BioGRID; 31243; 221.
DR DIP; DIP-6471N; -.
DR IntAct; P32892; 29.
DR MINT; P32892; -.
DR STRING; 4932.YLL008W; -.
DR iPTMnet; P32892; -.
DR MaxQB; P32892; -.
DR PaxDb; P32892; -.
DR PRIDE; P32892; -.
DR EnsemblFungi; YLL008W_mRNA; YLL008W; YLL008W.
DR GeneID; 850652; -.
DR KEGG; sce:YLL008W; -.
DR SGD; S000003931; DRS1.
DR VEuPathDB; FungiDB:YLL008W; -.
DR eggNOG; KOG0338; Eukaryota.
DR GeneTree; ENSGT00550000074997; -.
DR HOGENOM; CLU_003041_3_2_1; -.
DR InParanoid; P32892; -.
DR OMA; AAHTDIR; -.
DR BioCyc; YEAST:G3O-32113-MON; -.
DR PRO; PR:P32892; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32892; protein.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
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; ISA:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..752
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000055045"
FT DOMAIN 262..437
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 448..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 621..667
FT /evidence="ECO:0000255"
FT MOTIF 231..259
FT /note="Q motif"
FT MOTIF 385..388
FT /note="DEAD box"
FT COMPBIAS 119..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 191
FT /note="M->T: No growth at 13 degrees Celsius; when
FT associated with Q-431 and G-472."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 260
FT /note="A->V: No growth at 13 degrees Celsius; when
FT associated with P-564."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 273
FT /note="A->T: No growth at 13 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 288
FT /note="P->L: No growth at 13 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 291
FT /note="E->V: No growth at 13 degrees Celsius; when
FT associated with G-637."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 305
FT /note="V->D: No growth at 13 degrees Celsius; when
FT associated with V-306."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 306
FT /note="I->V: No growth at 13 degrees Celsius; when
FT associated with D-305."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 414
FT /note="L->S: No growth at 13 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 429
FT /note="L->P: No growth at 13 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 431
FT /note="L->Q: No growth at 13 degrees Celsius; when
FT associated with T-191 and G-472."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 472
FT /note="R->G: No growth at 13 degrees Celsius; when
FT associated with T-191 and Q-431."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 509
FT /note="L->S: No growth at 13 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 563
FT /note="Y->C: No growth at 13 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 564
FT /note="L->P: No growth at 13 degrees Celsius; when
FT associated with V-260."
FT /evidence="ECO:0000269|PubMed:11911362"
FT MUTAGEN 637
FT /note="D->G: No growth at 13 degrees Celsius; when
FT associated with V-291."
FT /evidence="ECO:0000269|PubMed:11911362"
SQ SEQUENCE 752 AA; 84843 MW; 60747607A6E5E4A8 CRC64;
MVVGTKKYSN LDFVPTISDS EDDVPILDSS DDEKVEAKKT TKKRKGKNNK KKVSEGDNLD
EDVHEDLDAG FKFDLDADDT TSNFQGWNFL AEGESNKDDA EAFVKKDVDL DKIIRRKGGL
VKMAHIDSKQ EEETEKEKVE KENDSDDEEL AMDGFGMGAP MNNGDENQSE EEEEEEEKEE
EEEEEEEQEE MTLEKGGKDD EIDEEDDSEE AKADFYAPET EGDEAKKQMY ENFNSLSLSR
PVLKGLASLG YVKPSPIQSA TIPIALLGKD IIAGAVTGSG KTAAFMIPII ERLLYKPAKI
ASTRVIVLLP TRELAIQVAD VGKQIARFVS GITFGLAVGG LNLRQQEQML KSRPDIVIAT
PGRFIDHIRN SASFNVDSVE ILVMDEADRM LEEGFQDELN EIMGLLPSNR QNLLFSATMN
SKIKSLVSLS LKKPVRIMID PPKKAATKLT QEFVRIRKRD HLKPALLFNL IRKLDPTGQK
RIVVFVARKE TAHRLRIIMG LLGMSVGELH GSLTQEQRLD SVNKFKNLEV PVLICTDLAS
RGLDIPKIEV VINYDMPKSY EIYLHRVGRT ARAGREGRSV TFVGESSQDR SIVRAAIKSV
EENKSLTQGK ALGRNVDWVQ IEETNKLVES MNDTIEDILV EEKEEKEILR AEMQLRKGEN
MLKHKKEIQA RPRRTWFQSE SDKKNSKVLG ALSRNKKVTN SKKRKREEAK ADGNGARSYR
KTKTDRIADQ ERTFKKQKST NSNKKKGFKS RR
