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Database: UniProt
Entry: P36009
LinkDB: P36009
Original site: P36009 
ID   DHR2_YEAST              Reviewed;         735 AA.
AC   P36009; D6VXK9; Q07040;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-OCT-2019, entry version 180.
DE   RecName: Full=Probable ATP-dependent RNA helicase DHR2;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box RNA helicase DHR2;
DE   AltName: Full=Helicase JA2;
GN   Name=DHR2; OrderedLocusNames=YKL078W; ORFNames=YKL408;
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].
RA   Arenas J.E., Messenger J.;
RT   "JA2: a DEAH family RNA-helicase-like gene from Saccharomyces
RT   cerevisiae.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Raju V.S., Datta P.K., Beales M.H., Ghoshal K., Jacob S.T.;
RT   "A clone isolated from a Clontech HeLa cDNA library has high homology
RT   to yeast DEAH helicases and hybridizes to Northern and Southern blots
RT   from yeast but not from HeLa.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8203165; DOI=10.1002/yea.320100211;
RA   James C.M., Gent M.E., Indge K.J., Oliver S.G.;
RT   "Sequence analysis of a 10 kb fragment of yeast chromosome XI
RT   identifies the SMY1 locus and reveals sequences related to a pre-mRNA
RT   splicing factor and vacuolar ATPase subunit C plus a number of
RT   unidentified open reading frames.";
RL   Yeast 10:247-255(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
RA   Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
RA   Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA   Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [5]
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   [6]
RP   CHARACTERIZATION.
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   [7]
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   [8]
RP   INTERACTION WITH NOP19.
RX   PubMed=21941128; DOI=10.4161/rna.8.6.17699;
RA   Choque E., Marcellin M., Burlet-Schiltz O., Gadal O., Dez C.;
RT   "The nucleolar protein Nop19p interacts preferentially with Utp25p and
RT   Dhr2p and is essential for the production of the 40S ribosomal subunit
RT   in Saccharomyces cerevisiae.";
RL   RNA Biol. 8:1158-1172(2011).
RN   [9]
RP   INTERACTION WITH UBP10.
RX   PubMed=22902402; DOI=10.1016/j.celrep.2012.07.009;
RA   Richardson L.A., Reed B.J., Charette J.M., Freed E.F.,
RA   Fredrickson E.K., Locke M.N., Baserga S.J., Gardner R.G.;
RT   "A conserved deubiquitinating enzyme controls cell growth by
RT   regulating RNA polymerase I stability.";
RL   Cell Rep. 2:372-385(2012).
RN   [10]
RP   INTERACTION WITH UBP10.
RX   PubMed=26149687; DOI=10.1074/jbc.m115.650952;
RA   Reed B.J., Locke M.N., Gardner R.G.;
RT   "A conserved deubiquitinating enzyme uses intrinsically disordered
RT   regions to scaffold multiple protein interaction sites.";
RL   J. Biol. Chem. 290:20601-20612(2015).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase. Required for 18S rRNA
CC       synthesis.
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 NOP19 (PubMed:21941128). Interacts with
CC       UBP10 (PubMed:22902402, PubMed:26149687).
CC       {ECO:0000269|PubMed:21941128, ECO:0000269|PubMed:22902402,
CC       ECO:0000269|PubMed:26149687}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-5844, EBI-5844;
CC       P38719:DBP8; NbExp=2; IntAct=EBI-5844, EBI-5633;
CC       P38333:ENP1; NbExp=2; IntAct=EBI-5844, EBI-6482;
CC       P53941:IMP4; NbExp=2; IntAct=EBI-5844, EBI-9243;
CC       P53317:NOP19; NbExp=3; IntAct=EBI-5844, EBI-23590;
CC       P53131:PRP43; NbExp=2; IntAct=EBI-5844, EBI-505;
CC       P40362:UTP18; NbExp=2; IntAct=EBI-5844, EBI-4534;
CC       P53254:UTP22; NbExp=3; IntAct=EBI-5844, EBI-1878;
CC       P40498:UTP25; NbExp=2; IntAct=EBI-5844, EBI-25113;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- MISCELLANEOUS: Present with 721 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}.
DR   EMBL; AF005090; AAB61670.1; -; Genomic_DNA.
DR   EMBL; L15328; AAA34986.1; -; Genomic_DNA.
DR   EMBL; X75560; CAA53239.1; -; Genomic_DNA.
DR   EMBL; Z28078; CAA81915.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09079.1; -; Genomic_DNA.
DR   PIR; S37903; S37903.
DR   RefSeq; NP_012845.1; NM_001179644.1.
DR   SMR; P36009; -.
DR   BioGrid; 34054; 266.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR   ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR   ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR   DIP; DIP-6424N; -.
DR   IntAct; P36009; 43.
DR   MINT; P36009; -.
DR   STRING; 4932.YKL078W; -.
DR   MaxQB; P36009; -.
DR   PaxDb; P36009; -.
DR   PRIDE; P36009; -.
DR   EnsemblFungi; YKL078W_mRNA; YKL078W; YKL078W.
DR   GeneID; 853784; -.
DR   KEGG; sce:YKL078W; -.
DR   EuPathDB; FungiDB:YKL078W; -.
DR   SGD; S000001561; DHR2.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; P36009; -.
DR   KO; K14781; -.
DR   OMA; RCYMRDL; -.
DR   BioCyc; YEAST:G3O-31873-MONOMER; -.
DR   PRO; PR:P36009; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0045943; P:positive regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0042254; P:ribosome biogenesis; IDA:SGD.
DR   GO; GO:0031167; P:rRNA methylation; TAS:Reactome.
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; 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; RNA-binding;
KW   rRNA processing.
FT   CHAIN         1    735       Probable ATP-dependent RNA helicase DHR2.
FT                                /FTId=PRO_0000055163.
FT   DOMAIN       91    257       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      262    456       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     104    111       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       203    206       DEAH box.
FT   CONFLICT     28     28       T -> M (in Ref. 2; AAA34986).
FT                                {ECO:0000305}.
FT   CONFLICT     80     98       TLPVYQHKREIMSYIESNP -> HFRLPTQARNNVIYSKQS
FT                                (in Ref. 2; AAA34986). {ECO:0000305}.
FT   CONFLICT    277    288       DAVIRCCIQINQ -> ALSSGVYTNKP (in Ref. 2;
FT                                AAA34986). {ECO:0000305}.
FT   CONFLICT    339    339       A -> P (in Ref. 2; AAA34986).
FT                                {ECO:0000305}.
SQ   SEQUENCE   735 AA;  82713 MW;  AAFA78B5F6215D89 CRC64;
     MAANSNSRVA SNHTSKKQKV RRNIHPFTNN TRIKRASKIV KFNDSGEGDH VSDQRSNKEN
     VLTYKSLKSR ASDLLKMRET LPVYQHKREI MSYIESNPVT VLIGETGSGK STQIPQFVLE
     KLYDTKKHGS IAVTQPRRVA AINLATRVAQ EHGCKLGEQV GYSVRFDNTT TTRTRLKYLT
     DGMLLRELMM NSDLREYSVI VIDEAHERTV LTDLILGFLK SLIQGPRPDL RIIVMSATLQ
     AEKFSEFFNN APILFVEGRK FDVKQYYLKA PTDDIVDAVI RCCIQINQGE ELGDILCFLP
     GQEEIDKAVT IMEKIAKYVS DEAPVPLIVP YPLYAALPAV QQSLVFAPIK GFKRKVVFST
     NIAETSVTIS GVKFVVDSGL RKVKVWRHQL GLATLLTVPI SQASAMQRSG RAGRESEGKS
     FRLYCESDYV KLPKQSEPEI ARSDVTSPVL MLKRYGVDDL LNWTWFENPG KEAIVMGLQE
     LYELGALDTR GKITKRGQQM ALLPLQPHLS SVLIKASEVG CLSQVIDIVS CLSVENLLLN
     PSPEERDEVN ERRLSLCNAG KRYGDLIMLK ELFDIYFYEL GKSQDASSER NDWCKGLCIS
     IRGFKNVIRV RDQLRVYCKR LFSSISEEDE ESKKIGEDGE LISKILKCFL TGFIKNTAIG
     MPDRSYRTVS TGEPISIHPS SMLFMNKSCP GIMYTEYVFT TKGYARNVSR IELSWLQEVV
     TNAAAVAKQK VSDSK
//
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