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Database: UniProt
Entry: Q04217
LinkDB: Q04217
Original site: Q04217 
ID   DHR1_YEAST              Reviewed;        1267 AA.
AC   Q04217; D6VZV1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   29-OCT-2014, entry version 135.
DE   RecName: Full=Probable ATP-dependent RNA helicase DHR1;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box RNA helicase DHR1;
DE   AltName: Full=Extracellular mutant protein 16;
GN   Name=ECM16; Synonyms=DHR1; OrderedLocusNames=YMR128W;
GN   ORFNames=YM9553.04;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
RP   FUNCTION, INTERACTION WITH SNORNA U3, AND SUBCELLULAR LOCATION.
RX   PubMed=10982841; DOI=10.1128/MCB.20.19.7238-7246.2000;
RA   Colley A., Beggs J.D., Tollervey D., Lafontaine D.L.J.;
RT   "Dhr1p, a putative DEAH-Box RNA helicase, is associated with the box
RT   C+D snoRNP U3.";
RL   Mol. Cell. Biol. 20:7238-7246(2000).
RN   [4]
RP   IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
RX   PubMed=12068309; DOI=10.1038/nature00769;
RA   Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA   Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E.,
RA   Shabanowitz J., Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT   "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT   biogenesis.";
RL   Nature 417:967-970(2002).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, 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: Probable ATP-binding RNA helicase. Required for 18S rRNA
CC       synthesis. May play a role in restructuring of the pre-rRNA.
CC       {ECO:0000269|PubMed:10982841}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Interacts with snoRNA U3. Component of the ribosomal
CC       small subunit (SSU) processome composed of at least 40 protein
CC       subunits and snoRNA U3. {ECO:0000269|PubMed:10982841,
CC       ECO:0000269|PubMed:12068309}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:10982841}.
CC   -!- MISCELLANEOUS: Present with 2000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00542}.
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DR   EMBL; Z48622; CAA88553.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10025.1; -; Genomic_DNA.
DR   PIR; S53058; S53058.
DR   RefSeq; NP_013847.1; NM_001182629.1.
DR   ProteinModelPortal; Q04217; -.
DR   SMR; Q04217; 383-642, 708-941.
DR   BioGrid; 35305; 85.
DR   DIP; DIP-6722N; -.
DR   IntAct; Q04217; 28.
DR   MINT; MINT-614026; -.
DR   STRING; 4932.YMR128W; -.
DR   MaxQB; Q04217; -.
DR   PaxDb; Q04217; -.
DR   PeptideAtlas; Q04217; -.
DR   PRIDE; Q04217; -.
DR   EnsemblFungi; YMR128W; YMR128W; YMR128W.
DR   GeneID; 855158; -.
DR   KEGG; sce:YMR128W; -.
DR   CYGD; YMR128w; -.
DR   SGD; S000004735; ECM16.
DR   eggNOG; COG1643; -.
DR   GeneTree; ENSGT00550000074985; -.
DR   HOGENOM; HOG000201240; -.
DR   InParanoid; Q04217; -.
DR   KO; K14780; -.
DR   OMA; QIRFEGT; -.
DR   OrthoDB; EOG79PJXZ; -.
DR   BioCyc; YEAST:G3O-32821-MONOMER; -.
DR   NextBio; 978575; -.
DR   Genevestigator; Q04217; -.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0042254; P:ribosome biogenesis; IDA:SGD.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN         1   1267       Probable ATP-dependent RNA helicase DHR1.
FT                                /FTId=PRO_0000055162.
FT   DOMAIN      401    580       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      675    858       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     414    421       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       516    519       DEAH box.
FT   MOD_RES     181    181       Phosphoserine.
FT                                {ECO:0000269|PubMed:19779198}.
SQ   SEQUENCE   1267 AA;  144955 MW;  576DAAE6D934CC77 CRC64;
     MGTYRKRFNE KARSGHMAKL KELKRIRNKQ FTRQDENDER VENPDSAPAE SSTTEPNANA
     EILEPLTEEE KKMKKRKLQE LFTPKESKVS RLKKKRLDKF IEHQLKREER KTIIGKLQDY
     KIDTSLLTSS KRLGEGRQTK KEEFKEALSL ERQGRGNEQT NEILYEEYEP KVWDEYGEGG
     SSEDDDGEDD FEASFGSMPK PTDNEEKKSS GFIDHRPAKF GGSGLSFGFS NIKVINKESK
     TPKKKYNWRQ RVEMEELKKH GKEDEMDFDT TSEDDDEEED QEEEDKMHPS ENPLEEVESA
     DSETGSEKFD QNDVANEFKD WANQEIKKLE GRDQELVTPT LNIDYKPIIR KEDLDDGLQE
     AYVPINENST RKAFYVEVSR SDEIQKARIQ LPVFGEEHKI MEAIHHNDVV IICGETGSGK
     TTQVPQFLYE AGFGAEDSPD YPGMVGITQP RRVAAVSMAE RVANELGDHG HKVGYQIRFD
     STAKEDTKVK FMTDGVLLRE MMHDFKLTKY SSIIIDEAHE RNINTDILIG MLSRCVRLRA
     KLHKENPIEH KKLKLIIMSA TLRVSDFSEN KTLFPIAPPV LQVDARQFPV SIHFNRRTAF
     NYTDEAFRKT CKIHQKLPPG AILVFLTGQQ EITHMVKRLR KEFPFKKNSK YNKDLETPVS
     KMGINSKTTD LEAEDIDFSV QVIDQDKFKS AIRYEEDEGN SGNGEDEEDE EEEGFEEVLT
     EGQTANDPLY VLPLYSLLPT KEQMRVFQKP PQGSRLCIVA TNVAETSLTI PGVRYVVDSG
     RSKERKYNES NGVQSFEVGW VSKASANQRS GRAGRTGPGH CYRLYSSAVF EHDFEQFSKP
     EILRMPVESI VLQMKSMAIH NIINFPFPTP PDRVALSKAI QLLQYLGALD NKEMITEDGK
     KMSLFPLSPR FSKMLLVSDE KACLPYIVAI VSALSVGDPF INEFELGINE ISRKPNPDEN
     LDDKIREHDE STPGMDPELK KELRSKFYKS RSQFSKLDKF SDVFRLLSVV SAMDYVPKEQ
     KEIFMKKNFL RGKLMEEIVK LRKQLMYIIK SNTSKENIAV VIRNEDLKSD IPSVIQIKLL
     KQMICAGFVD HVAVRADVLF PDDAKITNRT SIINIPYIPV LATRTPNIED CFVYIHPTSI
     LNNLGEMPPK YMLYYSLHLG GNNKTRMNTL CDIASTPLAN IARKGLLLTY SKPLTGQGLK
     TVNLSPTERY CYVVPRFGST VDNDLKIGWD LNPIAVHQKK QKGQWTVIKF ITRKGFQTIT
     GEEKEKK
//
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