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Database: UniProt
Entry: P20448
LinkDB: P20448
Original site: P20448 
ID   DBP4_YEAST              Reviewed;         770 AA.
AC   P20448; D6VWF0; Q6B1G2; Q92329;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   16-OCT-2019, entry version 185.
DE   RecName: Full=ATP-dependent RNA helicase HCA4;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 4;
DE   AltName: Full=Helicase CA4;
DE   AltName: Full=Helicase UF1;
GN   Name=HCA4; Synonyms=DBP4, ECM24; OrderedLocusNames=YJL033W;
GN   ORFNames=J1250;
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], AND FUNCTION.
RX   PubMed=9199348; DOI=10.1128/mcb.17.7.4124;
RA   Liang W.-Q., Clark J.A., Fournier M.J.;
RT   "The rRNA-processing function of the yeast U14 small nucleolar RNA can
RT   be rescued by a conserved RNA helicase-like protein.";
RL   Mol. Cell. Biol. 17:4124-4132(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-382.
RX   PubMed=2406722; DOI=10.1073/pnas.87.4.1571;
RA   Chang T.-H., Arenas J., Abelson J.;
RT   "Identification of five putative yeast RNA helicase genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
RA   Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
RA   Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
RA   Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of
RT   technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
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   [9]
RP   FUNCTION, INTERACTION WITH THE U3 AND U14 SNORNAS, ASSOCIATION WITH
RP   THE PRE-RIBOSOMAL COMPLEX, AND MUTAGENESIS OF LYS-91; SER-225 AND
RP   THR-227.
RX   PubMed=16209945; DOI=10.1016/j.molcel.2005.08.022;
RA   Kos M., Tollervey D.;
RT   "The putative RNA helicase Dbp4p is required for release of the U14
RT   snoRNA from preribosomes in Saccharomyces cerevisiae.";
RL   Mol. Cell 20:53-64(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [11]
RP   FUNCTION, RNA-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18975973; DOI=10.1021/bi8016119;
RA   Garcia I., Uhlenbeck O.C.;
RT   "Differential RNA-dependent ATPase activities of four rRNA processing
RT   yeast DEAD-box proteins.";
RL   Biochemistry 47:12562-12573(2008).
RN   [12]
RP   FUNCTION.
RX   PubMed=18833290; DOI=10.1038/embor.2008.184;
RA   Bohnsack M.T., Kos M., Tollervey D.;
RT   "Quantitative analysis of snoRNA association with pre-ribosomes and
RT   release of snR30 by Rok1 helicase.";
RL   EMBO Rep. 9:1230-1236(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710; SER-714 AND
RP   SER-743, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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: ATP-dependent RNA helicase required for ribosome
CC       biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal
CC       complexes. Required for pre-rRNA cleavage at site A2.
CC       {ECO:0000269|PubMed:16209945, ECO:0000269|PubMed:18833290,
CC       ECO:0000269|PubMed:18975973, ECO:0000269|PubMed:9199348}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.24 mM for ATP {ECO:0000269|PubMed:18975973};
CC   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with
CC       pre-ribosomal complexes. {ECO:0000269|PubMed:16209945}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-5612, EBI-5612;
CC       Q06631:BFR2; NbExp=5; IntAct=EBI-5612, EBI-36432;
CC       P15790:CKA1; NbExp=2; IntAct=EBI-5612, EBI-9533;
CC       P48234:ENP2; NbExp=3; IntAct=EBI-5612, EBI-23354;
CC       Q06344:ESF1; NbExp=3; IntAct=EBI-5612, EBI-34121;
CC       P53743:ESF2; NbExp=2; IntAct=EBI-5612, EBI-28537;
CC       Q03532:HAS1; NbExp=3; IntAct=EBI-5612, EBI-8170;
CC       Q12136:SAS10; NbExp=3; IntAct=EBI-5612, EBI-36084;
CC       P53254:UTP22; NbExp=3; IntAct=EBI-5612, EBI-1878;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- MISCELLANEOUS: Present with 7900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
DR   EMBL; U72149; AAB17005.1; -; Genomic_DNA.
DR   EMBL; Z49308; CAA89324.1; -; Genomic_DNA.
DR   EMBL; AY693118; AAT93137.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08766.1; -; Genomic_DNA.
DR   PIR; S56805; S56805.
DR   RefSeq; NP_012501.1; NM_001181467.1.
DR   SMR; P20448; -.
DR   BioGrid; 33727; 189.
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-6819N; -.
DR   IntAct; P20448; 62.
DR   MINT; P20448; -.
DR   STRING; 4932.YJL033W; -.
DR   iPTMnet; P20448; -.
DR   MaxQB; P20448; -.
DR   PaxDb; P20448; -.
DR   PRIDE; P20448; -.
DR   EnsemblFungi; YJL033W_mRNA; YJL033W; YJL033W.
DR   GeneID; 853419; -.
DR   KEGG; sce:YJL033W; -.
DR   EuPathDB; FungiDB:YJL033W; -.
DR   SGD; S000003570; HCA4.
DR   HOGENOM; HOG000268801; -.
DR   InParanoid; P20448; -.
DR   KO; K14776; -.
DR   OMA; KVRTKYD; -.
DR   BioCyc; YEAST:G3O-31500-MONOMER; -.
DR   PRO; PR:P20448; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   GO; GO:0005730; C:nucleolus; IC:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; IMP:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034512; F:box C/D snoRNA binding; IDA:SGD.
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:0008186; F:RNA-dependent ATPase activity; IDA:SGD.
DR   GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN         1    770       ATP-dependent RNA helicase HCA4.
FT                                /FTId=PRO_0000055018.
FT   DOMAIN       72    246       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      278    437       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      85     92       ATP.
FT   MOTIF        41     69       Q motif.
FT   MOTIF       194    197       DEAD box.
FT   MOD_RES     692    692       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956}.
FT   MOD_RES     710    710       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     714    714       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     743    743       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN      91     91       K->A,R: Lethal and prevents release of
FT                                U14 snoRNA from pre-ribosomes.
FT                                {ECO:0000269|PubMed:16209945}.
FT   MUTAGEN     225    225       S->A: Lethal and prevents release of U14
FT                                snoRNA from pre-ribosomes; when
FT                                associated with A-227.
FT                                {ECO:0000269|PubMed:16209945}.
FT   MUTAGEN     227    227       T->A: Lethal and prevents release of U14
FT                                snoRNA from pre-ribosomes; when
FT                                associated with A-225.
FT                                {ECO:0000269|PubMed:16209945}.
FT   CONFLICT     36     36       K -> R (in Ref. 4; AAT93137).
FT                                {ECO:0000305}.
FT   CONFLICT    381    381       V -> I (in Ref. 5; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    465    465       Q -> E (in Ref. 1; AAB17005).
FT                                {ECO:0000305}.
FT   CONFLICT    512    512       F -> L (in Ref. 1; AAB17005).
FT                                {ECO:0000305}.
FT   CONFLICT    668    673       KQEKKR -> NKRRRG (in Ref. 1; AAB17005).
FT                                {ECO:0000305}.
FT   CONFLICT    675    675       R -> D (in Ref. 1; AAB17005).
FT                                {ECO:0000305}.
SQ   SEQUENCE   770 AA;  87193 MW;  0C9E4DEF5BFD640E CRC64;
     MAKKNRLNTT QRKTLRQKED EYIENLKTKI DEYDPKITKA KFFKDLPISD PTLKGLRESS
     FIKLTEIQAD SIPVSLQGHD VLAAAKTGSG KTLAFLVPVI EKLYREKWTE FDGLGALIIS
     PTRELAMQIY EVLTKIGSHT SFSAGLVIGG KDVKFELERI SRINILIGTP GRILQHLDQA
     VGLNTSNLQM LVLDEADRCL DMGFKKTLDA IVSTLSPSRQ TLLFSATQSQ SVADLARLSL
     TDYKTVGTHD VMDGSVNKEA STPETLQQFY IEVPLADKLD ILFSFIKSHL KCKMIVFLSS
     SKQVHFVYET FRKMQPGISL MHLHGRQKQR ARTETLDKFN RAQQVCLFAT DVVARGIDFP
     AVDWVVQVDC PEDVDTYIHR VGRCARYGKK GKSLIMLTPQ EQEAFLKRLN ARKIEPGKLN
     IKQSKKKSIK PQLQSLLFKD PELKYLGQKA FISYVRSIYV QKDKQVFKFD ELPTEEFAYS
     LGLPGAPKIK MKGMKTIEQA KERKNAPRQL AFLSKANEDG EVIEDKSKQP RTKYDKMFER
     KNQTILSEHY LNITKAQAQE DEDDDFISVK RKDHEINEAE LPALTLPTSR RAQKKALSKK
     ASLASKGNAS KLIFDDEGEA HPVYELEDEE EFHKRGDAEV QKTEFLTKES AVMADIDNID
     KQVAKEKKQE KKRKRLEAMR REMEAAMEEE ISGDEEEGKT VAYLGTGNLS DDMSDGDMPD
     SEGHLKKKAR TVDYSHGHNP SNSVDDDIIE VEEPQTLEDL ESLTAKLIQG
//
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