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   02-SEP-2026, entry version 210.
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 + phosphate + H(+); 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; P53874: UBP10; NbExp=2; IntAct=EBI-5844, EBI-19873;
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; 303.
DR   DIP; DIP-6424N; -.
DR   FunCoup; P36009; 260.
DR   IntAct; P36009; 45.
DR   MINT; P36009; -.
DR   STRING; 4932.YKL078W; -.
DR   iPTMnet; P36009; -.
DR   PaxDb; 4932-YKL078W; -.
DR   PeptideAtlas; P36009; -.
DR   EnsemblFungi; YKL078W_mRNA; YKL078W; YKL078W.
DR   GeneID; 853784; -.
DR   KEGG; sce:YKL078W; -.
DR   AGR; SGD:S000001561; -.
DR   SGD; S000001561; DHR2.
DR   VEuPathDB; FungiDB:YKL078W; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; P36009; -.
DR   OMA; APVHDFV; -.
DR   OrthoDB; 10253254at2759; -.
DR   BioCyc; YEAST:G3O-31873-MONOMER; -.
DR   BioGRID-ORCS; 853784; 6 hits in 10 CRISPR screens.
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:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-ARBA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   FunFam; 1.20.120.1080:FF:000028; ATP-dependent RNA helicase; 1.
DR   FunFam; 3.40.50.300:FF:002124; ATP-dependent RNA helicase; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF04408; WHD_HA2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   COMPBIAS        1..13
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..24
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//