ID DBP8_YEAST Reviewed; 431 AA.
AC P38719; D3DLB8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 195.
DE RecName: Full=ATP-dependent RNA helicase DBP8;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 8;
GN Name=DBP8; OrderedLocusNames=YHR169W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 51-GLY-LYS-52;
RP 155-ASP-GLU-156; 188-THR--THR-190 AND 341-ARG-SER-342.
RX PubMed=11222764; DOI=10.1093/nar/29.5.1144;
RA Daugeron M.-C., Linder P.;
RT "Characterization and mutational analysis of yeast Dbp8p, a putative RNA
RT helicase involved in ribosome biogenesis.";
RL Nucleic Acids Res. 29:1144-1155(2001).
RN [4]
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 [5]
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 [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH ESF2, AND
RP MUTAGENESIS OF LYS-52 AND ASP-155.
RX PubMed=16772403; DOI=10.1093/nar/gkl419;
RA Granneman S., Lin C., Champion E.A., Nandineni M.R., Zorca C.,
RA Baserga S.J.;
RT "The nucleolar protein Esf2 interacts directly with the DExD/H box RNA
RT helicase, Dbp8, to stimulate ATP hydrolysis.";
RL Nucleic Acids Res. 34:3189-3199(2006).
CC -!- FUNCTION: ATP-binding RNA helicase involved in 40S ribosomal subunit
CC biogenesis and is required for the normal formation of 18S rRNAs
CC through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC vegetative growth. {ECO:0000269|PubMed:11222764,
CC ECO:0000269|PubMed:16772403}.
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 pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:16772403};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:16772403};
CC -!- SUBUNIT: Interacts with ESF2. {ECO:0000269|PubMed:16772403}.
CC -!- INTERACTION:
CC P38719; P36009: DHR2; NbExp=2; IntAct=EBI-5633, EBI-5844;
CC P38719; P53743: ESF2; NbExp=4; IntAct=EBI-5633, EBI-28537;
CC P38719; P53254: UTP22; NbExp=2; IntAct=EBI-5633, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11222764,
CC ECO:0000269|PubMed:14562095}.
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 -!- MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX49/DBP8
CC subfamily. {ECO:0000305}.
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DR EMBL; U00027; AAB68014.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06862.1; -; Genomic_DNA.
DR PIR; S48908; S48908.
DR RefSeq; NP_012039.1; NM_001179300.1.
DR AlphaFoldDB; P38719; -.
DR SMR; P38719; -.
DR BioGRID; 36603; 120.
DR DIP; DIP-5628N; -.
DR IntAct; P38719; 87.
DR MINT; P38719; -.
DR STRING; 4932.YHR169W; -.
DR MaxQB; P38719; -.
DR PaxDb; 4932-YHR169W; -.
DR PeptideAtlas; P38719; -.
DR EnsemblFungi; YHR169W_mRNA; YHR169W; YHR169W.
DR GeneID; 856574; -.
DR KEGG; sce:YHR169W; -.
DR AGR; SGD:S000001212; -.
DR SGD; S000001212; DBP8.
DR VEuPathDB; FungiDB:YHR169W; -.
DR eggNOG; KOG0340; Eukaryota.
DR GeneTree; ENSGT00730000111231; -.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; P38719; -.
DR OMA; IAAETRW; -.
DR OrthoDB; 149428at2759; -.
DR BioCyc; YEAST:G3O-31203-MONOMER; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 856574; 8 hits in 10 CRISPR screens.
DR PRO; PR:P38719; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38719; Protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IMP:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd17955; DEADc_DDX49; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF21; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..431
FT /note="ATP-dependent RNA helicase DBP8"
FT /id="PRO_0000055038"
FT DOMAIN 33..209
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 242..389
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 404..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..30
FT /note="Q motif"
FT MOTIF 155..158
FT /note="DEAD box"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 51..52
FT /note="GK->AA: In DBP8-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:11222764"
FT MUTAGEN 52
FT /note="K->A,R: Decreases ATPase activity in vitro."
FT /evidence="ECO:0000269|PubMed:16772403"
FT MUTAGEN 155..156
FT /note="DE->AA: In DBP8-2; loss of activity."
FT /evidence="ECO:0000269|PubMed:11222764"
FT MUTAGEN 155
FT /note="D->A: Decreases ATPase activity in vitro."
FT /evidence="ECO:0000269|PubMed:16772403"
FT MUTAGEN 188..190
FT /note="TAT->AAA: In DBP8-3; severely affects growth."
FT /evidence="ECO:0000269|PubMed:11222764"
FT MUTAGEN 341..342
FT /note="RS->AA: In DBP8-4; no effect on growth."
FT /evidence="ECO:0000269|PubMed:11222764"
SQ SEQUENCE 431 AA; 47878 MW; B0451EB85247372C CRC64;
MADFKSLGLS KWLTESLRAM KITQPTAIQK ACIPKILEGR DCIGGAKTGS GKTIAFAGPM
LTKWSEDPSG MFGVVLTPTR ELAMQIAEQF TALGSSMNIR VSVIVGGESI VQQALDLQRK
PHFIIATPGR LAHHIMSSGD DTVGGLMRAK YLVLDEADIL LTSTFADHLA TCISALPPKD
KRQTLLFTAT ITDQVKSLQN APVQKGKPPL FAYQVESVDN VAIPSTLKIE YILVPEHVKE
AYLYQLLTCE EYENKTAIIF VNRTMTAEIL RRTLKQLEVR VASLHSQMPQ QERTNSLHRF
RANAARILIA TDVASRGLDI PTVELVVNYD IPSDPDVFIH RSGRTARAGR IGDAISFVTQ
RDVSRIQAIE DRINKKMTET NKVHDTAVIR KALTKVTKAK RESLMAMQKE NFGERKRQQK
KKQNDGKSLR S
//
