DBP10_YEAST
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 03-AUG-2022, entry version 197.
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; Saccharomycetes;
OC 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 from
RT Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames
RT (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1
RT 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 required
RT 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 BY
RP 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 SER-400, AND
RP IDENTIFICATION 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 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 Q12389; Q12389: DBP10; NbExp=3; IntAct=EBI-5644, EBI-5644;
CC Q12389; P32892: DRS1; NbExp=4; IntAct=EBI-5644, EBI-6170;
CC Q12389; P36049: EBP2; NbExp=3; IntAct=EBI-5644, EBI-6289;
CC Q12389; Q03532: HAS1; NbExp=4; IntAct=EBI-5644, EBI-8170;
CC Q12389; P43586: LOC1; NbExp=5; IntAct=EBI-5644, EBI-22906;
CC Q12389; Q12176: MAK21; NbExp=3; IntAct=EBI-5644, EBI-10944;
CC Q12389; P38112: MAK5; NbExp=3; IntAct=EBI-5644, EBI-10394;
CC Q12389; P39744: NOC2; NbExp=5; IntAct=EBI-5644, EBI-29259;
CC Q12389; P37838: NOP4; NbExp=3; IntAct=EBI-5644, EBI-12122;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10871363}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000305}.
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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 AlphaFoldDB; Q12389; -.
DR SMR; Q12389; -.
DR BioGRID; 32025; 276.
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 SGD; S000002189; DBP10.
DR VEuPathDB; FungiDB:YDL031W; -.
DR eggNOG; KOG0337; Eukaryota.
DR GeneTree; ENSGT00550000075100; -.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; Q12389; -.
DR OMA; MRWDKKS; -.
DR BioCyc; YEAST:G3O-29457-MON; -.
DR PRO; PR:Q12389; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12389; protein.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..995
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000055040"
FT DOMAIN 168..340
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 418..568
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..165
FT /note="Q motif"
FT MOTIF 288..291
FT /note="DEAD box"
FT COMPBIAS 38..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 733..741
FT /note="SHSIEDEIL -> HILSKMKFW (in Ref. 1; CAA96458 and 2;
FT CAA98590)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="G -> V (in Ref. 1; CAA96458 and 2; CAA98590)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="D -> H (in Ref. 1; CAA96458 and 2; CAA98590)"
FT /evidence="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
