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Database: UniProt
Entry: P32892
LinkDB: P32892
Original site: P32892 
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   16-OCT-2019, entry version 181.
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;
OC   Saccharomycetes; 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
RT   cerevisiae 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
RT   a 43.7 kb fragment of chromosome XII including an open reading frame
RT   homologous to the human cystic fibrosis transmembrane conductance
RT   regulator 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.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   FUNCTION.
RX   PubMed=8247005; DOI=10.1128/mcb.13.12.7901;
RA   Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.;
RT   "DRS1 to DRS7, novel genes required for ribosome assembly and function
RT   in 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;
RP   GLU-291; VAL-305; ILE-306; LEU-414; LEU-429; LEU-431; ARG-472;
RP   LEU-509; TYR-563; 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
RP   BY 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION
RP   BY 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
RT   insights 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       Q12389:DBP10; NbExp=4; IntAct=EBI-6170, EBI-5644;
CC       Q04660:ERB1; NbExp=4; IntAct=EBI-6170, EBI-28098;
CC       P43586:LOC1; NbExp=4; IntAct=EBI-6170, EBI-22906;
CC       P37838:NOP4; NbExp=4; IntAct=EBI-6170, EBI-12122;
CC       P40693:RLP7; NbExp=3; IntAct=EBI-6170, EBI-15415;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:1454790, ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       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};
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   SMR; P32892; -.
DR   BioGrid; 31243; 193.
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   EuPathDB; FungiDB:YLL008W; -.
DR   SGD; S000003931; DRS1.
DR   HOGENOM; HOG000265456; -.
DR   InParanoid; P32892; -.
DR   KO; K13181; -.
DR   OMA; HEPERSW; -.
DR   BioCyc; YEAST:G3O-32113-MONOMER; -.
DR   PRO; PR:P32892; -.
DR   Proteomes; UP000002311; Chromosome XII.
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:0003723; F:RNA binding; IBA:GO_Central.
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   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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding.
FT   CHAIN         1    752       ATP-dependent RNA helicase DRS1.
FT                                /FTId=PRO_0000055045.
FT   DOMAIN      262    437       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      448    639       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     275    282       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      621    667       {ECO:0000255}.
FT   MOTIF       231    259       Q motif.
FT   MOTIF       385    388       DEAD box.
FT   COMPBIAS    170    190       Poly-Glu.
FT   MOD_RES     208    208       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MUTAGEN     191    191       M->T: No growth at 13 degrees Celsius;
FT                                when associated with Q-431 and G-472.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     260    260       A->V: No growth at 13 degrees Celsius;
FT                                when associated with P-564.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     273    273       A->T: No growth at 13 degrees Celsius.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     288    288       P->L: No growth at 13 degrees Celsius.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     291    291       E->V: No growth at 13 degrees Celsius;
FT                                when associated with G-637.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     305    305       V->D: No growth at 13 degrees Celsius;
FT                                when associated with V-306.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     306    306       I->V: No growth at 13 degrees Celsius;
FT                                when associated with D-305.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     414    414       L->S: No growth at 13 degrees Celsius.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     429    429       L->P: No growth at 13 degrees Celsius.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     431    431       L->Q: No growth at 13 degrees Celsius;
FT                                when associated with T-191 and G-472.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     472    472       R->G: No growth at 13 degrees Celsius;
FT                                when associated with T-191 and Q-431.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     509    509       L->S: No growth at 13 degrees Celsius.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     563    563       Y->C: No growth at 13 degrees Celsius.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     564    564       L->P: No growth at 13 degrees Celsius;
FT                                when associated with V-260.
FT                                {ECO:0000269|PubMed:11911362}.
FT   MUTAGEN     637    637       D->G: No growth at 13 degrees Celsius;
FT                                when associated with V-291.
FT                                {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
//
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