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 01-MAY-2013, entry version 122.
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 204511 / S288c / AB972;
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;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Probable ATP-binding RNA helicase. Required for 18S rRNA
CC synthesis. May play a role in restructuring of the pre-rRNA.
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.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- MISCELLANEOUS: Present with 2000 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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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 DIP; DIP-6722N; -.
DR IntAct; Q04217; 28.
DR MINT; MINT-614026; -.
DR STRING; 4932.YMR128W; -.
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 KO; K14780; -.
DR OMA; HQLKREE; -.
DR OrthoDB; EOG4KM2B8; -.
DR NextBio; 978575; -.
DR Genevestigator; Q04217; -.
DR GermOnline; YMR128W; Saccharomyces cerevisiae.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
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 InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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 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 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; Reference proteome; Ribonucleoprotein;
KW 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 DOMAIN 675 858 Helicase C-terminal.
FT NP_BIND 414 421 ATP (By similarity).
FT MOTIF 516 519 DEAH box.
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
//
