GenomeNet

Database: UniProt
Entry: Q12389
LinkDB: Q12389
Original site: Q12389 
ID   DBP10_YEAST             Reviewed;         995 AA.
AC   Q12389; D6VRW1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   13-NOV-2019, entry version 183.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 10;
GN   Name=DBP10; OrderedLocusNames=YDL031W; ORFNames=D2770;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9046088;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<65::aid-yea50>3.0.co;2-t;
RA   Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
RT   "The sequence of a 36.7 kb segment on the left arm of chromosome IV
RT   from Saccharomyces cerevisiae reveals 20 non-overlapping open reading
RT   frames (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9,
RT   ACT2 and MPS1 and 11 new ORFs.";
RL   Yeast 13:65-71(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 733-741; 746 AND 764.
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10871363; DOI=10.1093/nar/28.12.2315;
RA   Burger F., Daugeron M.-C., Linder P.;
RT   "Dbp10p, a putative RNA helicase from Saccharomyces cerevisiae, is
RT   required for ribosome biogenesis.";
RL   Nucleic Acids Res. 28:2315-2323(2000).
RN   [5]
RP   INTERACTION WITH RRP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15100437; DOI=10.1261/rna.5255804;
RA   Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA   Woolford J.L. Jr.;
RT   "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT   maturation.";
RL   RNA 10:813-827(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-398 AND
RP   SER-400, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE 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-binding RNA helicase involved in the biogenesis of
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 5.8S rRNAs. {ECO:0000269|PubMed:10871363}.
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 RRP1 and associates with pre-ribosomal
CC       particles. {ECO:0000269|PubMed:15100437}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-5644, EBI-5644;
CC       P32892:DRS1; NbExp=4; IntAct=EBI-5644, EBI-6170;
CC       P36049:EBP2; NbExp=3; IntAct=EBI-5644, EBI-6289;
CC       Q03532:HAS1; NbExp=4; IntAct=EBI-5644, EBI-8170;
CC       P43586:LOC1; NbExp=5; IntAct=EBI-5644, EBI-22906;
CC       Q12176:MAK21; NbExp=3; IntAct=EBI-5644, EBI-10944;
CC       P38112:MAK5; NbExp=3; IntAct=EBI-5644, EBI-10394;
CC       P39744:NOC2; NbExp=5; IntAct=EBI-5644, EBI-29259;
CC       P37838:NOP4; NbExp=3; IntAct=EBI-5644, EBI-12122;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:10871363}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
DR   EMBL; Z71781; CAA96458.1; -; Genomic_DNA.
DR   EMBL; Z74079; CAA98590.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11821.2; -; Genomic_DNA.
DR   PIR; S67564; S67564.
DR   RefSeq; NP_010253.2; NM_001180090.2.
DR   SMR; Q12389; -.
DR   BioGrid; 32025; 250.
DR   DIP; DIP-6387N; -.
DR   IntAct; Q12389; 33.
DR   MINT; Q12389; -.
DR   STRING; 4932.YDL031W; -.
DR   iPTMnet; Q12389; -.
DR   MaxQB; Q12389; -.
DR   PaxDb; Q12389; -.
DR   PRIDE; Q12389; -.
DR   EnsemblFungi; YDL031W_mRNA; YDL031W; YDL031W.
DR   GeneID; 851530; -.
DR   KEGG; sce:YDL031W; -.
DR   EuPathDB; FungiDB:YDL031W; -.
DR   SGD; S000002189; DBP10.
DR   HOGENOM; HOG000246455; -.
DR   InParanoid; Q12389; -.
DR   KO; K14808; -.
DR   OMA; CVEMDLK; -.
DR   BioCyc; YEAST:G3O-29457-MONOMER; -.
DR   PRO; PR:Q12389; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IGI:SGD.
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; ISS:SGD.
DR   GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IMP:SGD.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   InterPro; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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   PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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    995       ATP-dependent RNA helicase DBP10.
FT                                /FTId=PRO_0000055040.
FT   DOMAIN      168    340       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      418    568       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     181    188       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       137    165       Q motif.
FT   MOTIF       288    291       DEAD box.
FT   MOD_RES     101    101       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     398    398       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MOD_RES     400    400       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   CONFLICT    733    741       SHSIEDEIL -> HILSKMKFW (in Ref. 1;
FT                                CAA96458 and 2; CAA98590). {ECO:0000305}.
FT   CONFLICT    746    746       G -> V (in Ref. 1; CAA96458 and 2;
FT                                CAA98590). {ECO:0000305}.
FT   CONFLICT    764    764       D -> H (in Ref. 1; CAA96458 and 2;
FT                                CAA98590). {ECO:0000305}.
SQ   SEQUENCE   995 AA;  112946 MW;  0533013C276095DF CRC64;
     MAGVQKRKRD LEDQDDNGSE EDDIAFDIAN EIALNDSESD ANDSDSEVEA DYGPNDVQDV
     IEYSSDEEEG VNNKKKAENK DIKKKKNSKK EIAAFPMLEM SDDENNASGK TQTGDDEDDV
     NEYFSTNNLE KTKHKKGSFP SFGLSKIVLN NIKRKGFRQP TPIQRKTIPL ILQSRDIVGM
     ARTGSGKTAA FILPMVEKLK SHSGKIGARA VILSPSRELA MQTFNVFKDF ARGTELRSVL
     LTGGDSLEEQ FGMMMTNPDV IIATPGRFLH LKVEMNLDLK SVEYVVFDEA DRLFEMGFQE
     QLNELLASLP TTRQTLLFSA TLPNSLVDFV KAGLVNPVLV RLDAETKVSE NLEMLFLSSK
     NADREANLLY ILQEIIKIPL ATSEQLQKLQ NSNNEADSDS DDENDRQKKR RNFKKEKFRK
     QKMPAANELP SEKATILFVP TRHHVEYISQ LLRDCGYLIS YIYGTLDQHA RKRQLYNFRA
     GLTSILVVTD VAARGVDIPM LANVINYTLP GSSKIFVHRV GRTARAGNKG WAYSIVAENE
     LPYLLDLELF LGKKILLTPM YDSLVDVMKK RWIDEGKPEY QFQPPKLSYT KRLVLGSCPR
     LDVEGLGDLY KNLMSSNFDL QLAKKTAMKA EKLYYRTRTS ASPESLKRSK EIISSGWDAQ
     NAFFGKNEEK EKLDFLAKLQ NRRNKETVFE FTRNPDDEMA VFMKRRRKQL APIQRKATER
     RELLEKERMA GLSHSIEDEI LKGDDGETGY TVSEDALKEF EDADQLLEAQ ENENKKKKKP
     KSFKDPTFFL SHYAPAGDIQ DKQLQITNGF ANDAAQAAYD LNSDDKVQVH KQTATVKWDK
     KRKKYVNTQG IDNKKYIIGE SGQKIAASFR SGRFDDWSKA RNLKPLKVGS RETSIPSNLL
     EDPSQGPAAN GRTVRGKFKH KQMKAPKMPD KHRDNYYSQK KKVEKALQSG ISVKGYNNAP
     GLRSELKSTE QIRKDRIIAE KKRAKNARPS KKRKF
//
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