DHR2_YEAST
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 03-AUG-2022, entry version 193.
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; Saccharomycetes;
OC 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 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 to
RT yeast DEAH helicases and hybridizes to Northern and Southern blots from
RT 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 identifies
RT the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor
RT and vacuolar ATPase subunit C plus a number of unidentified open reading
RT 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., Bossier P.,
RA 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., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 C+D
RT 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., Dephoure N.,
RA 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 in
RT 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., Fredrickson E.K.,
RA Locke M.N., Baserga S.J., Gardner R.G.;
RT "A conserved deubiquitinating enzyme controls cell growth by regulating RNA
RT 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 regions
RT 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 UBP10
CC (PubMed:22902402, PubMed:26149687). {ECO:0000269|PubMed:21941128,
CC ECO:0000269|PubMed:22902402, ECO:0000269|PubMed:26149687}.
CC -!- INTERACTION:
CC P36009; P38719: DBP8; NbExp=2; IntAct=EBI-5844, EBI-5633;
CC P36009; P36009: DHR2; NbExp=2; IntAct=EBI-5844, EBI-5844;
CC P36009; P38333: ENP1; NbExp=2; IntAct=EBI-5844, EBI-6482;
CC P36009; P53941: IMP4; NbExp=2; IntAct=EBI-5844, EBI-9243;
CC P36009; P53317: NOP19; NbExp=3; IntAct=EBI-5844, EBI-23590;
CC P36009; P53131: PRP43; NbExp=2; IntAct=EBI-5844, EBI-505;
CC P36009; P40362: UTP18; NbExp=2; IntAct=EBI-5844, EBI-4534;
CC P36009; P53254: UTP22; NbExp=3; IntAct=EBI-5844, EBI-1878;
CC P36009; 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 medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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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 AlphaFoldDB; P36009; -.
DR SMR; P36009; -.
DR BioGRID; 34054; 293.
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 SGD; S000001561; DHR2.
DR VEuPathDB; FungiDB:YKL078W; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000156747; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; P36009; -.
DR OMA; HIHRTTP; -.
DR BioCyc; YEAST:G3O-31873-MON; -.
DR PRO; PR:P36009; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36009; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
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 Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..735
FT /note="Probable ATP-dependent RNA helicase DHR2"
FT /id="PRO_0000055163"
FT DOMAIN 91..257
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 262..456
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 203..206
FT /note="DEAH box"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 28
FT /note="T -> M (in Ref. 2; AAA34986)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..98
FT /note="TLPVYQHKREIMSYIESNP -> HFRLPTQARNNVIYSKQS (in Ref.
FT 2; AAA34986)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..288
FT /note="DAVIRCCIQINQ -> ALSSGVYTNKP (in Ref. 2; AAA34986)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> P (in Ref. 2; AAA34986)"
FT /evidence="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
