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P38719 (DBP8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase DBP8

EC=3.6.4.13
Alternative name(s):
DEAD box protein 8
Gene names
Name:DBP8
Ordered Locus Names:YHR169W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth. Ref.3 Ref.6

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with ESF2. Ref.6

Subcellular location

Nucleusnucleolus Ref.3 Ref.4.

Domain

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Miscellaneous

Present with 3500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.4. Ref.6

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431ATP-dependent RNA helicase DBP8
PRO_0000055038

Regions

Domain33 – 209177Helicase ATP-binding
Domain242 – 389148Helicase C-terminal
Nucleotide binding46 – 538ATP
Motif2 – 3029Q motif
Motif155 – 1584DEAD box

Experimental info

Mutagenesis51 – 522GK → AA in DBP8-1; loss of activity. Ref.6
Mutagenesis521K → A or R: Decreases ATPase activity in vitro. Ref.6
Mutagenesis155 – 1562DE → AA in DBP8-2; loss of activity. Ref.6
Mutagenesis1551D → A: Decreases ATPase activity in vitro. Ref.6
Mutagenesis188 – 1903TAT → AAA in DBP8-3; severely affects growth. Ref.3
Mutagenesis341 – 3422RS → AA in DBP8-4; no effect on growth.

Sequences

Sequence LengthMass (Da)Tools
P38719 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B0451EB85247372C

FASTA43147,878
        10         20         30         40         50         60 
MADFKSLGLS KWLTESLRAM KITQPTAIQK ACIPKILEGR DCIGGAKTGS GKTIAFAGPM 

        70         80         90        100        110        120 
LTKWSEDPSG MFGVVLTPTR ELAMQIAEQF TALGSSMNIR VSVIVGGESI VQQALDLQRK 

       130        140        150        160        170        180 
PHFIIATPGR LAHHIMSSGD DTVGGLMRAK YLVLDEADIL LTSTFADHLA TCISALPPKD 

       190        200        210        220        230        240 
KRQTLLFTAT ITDQVKSLQN APVQKGKPPL FAYQVESVDN VAIPSTLKIE YILVPEHVKE 

       250        260        270        280        290        300 
AYLYQLLTCE EYENKTAIIF VNRTMTAEIL RRTLKQLEVR VASLHSQMPQ QERTNSLHRF 

       310        320        330        340        350        360 
RANAARILIA TDVASRGLDI PTVELVVNYD IPSDPDVFIH RSGRTARAGR IGDAISFVTQ 

       370        380        390        400        410        420 
RDVSRIQAIE DRINKKMTET NKVHDTAVIR KALTKVTKAK RESLMAMQKE NFGERKRQQK 

       430 
KKQNDGKSLR S 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Characterization and mutational analysis of yeast Dbp8p, a putative RNA helicase involved in ribosome biogenesis."
Daugeron M.-C., Linder P.
Nucleic Acids Res. 29:1144-1155(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 51-GLY-LYS-52; 155-ASP-GLU-156; 188-THR--THR-190 AND 341-ARG-SER-342.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis."
Granneman S., Lin C., Champion E.A., Nandineni M.R., Zorca C., Baserga S.J.
Nucleic Acids Res. 34:3189-3199(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH ESF2, MUTAGENESIS OF LYS-52 AND ASP-155.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00027 Genomic DNA. Translation: AAB68014.1.
BK006934 Genomic DNA. Translation: DAA06862.1.
PIRS48908.
RefSeqNP_012039.1. NM_001179300.1.

3D structure databases

ProteinModelPortalP38719.
SMRP38719. Positions 4-404.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5628N.
IntActP38719. 73 interactions.
MINTMINT-485349.
STRING4932.YHR169W.

Proteomic databases

PaxDbP38719.
PeptideAtlasP38719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR169W; YHR169W; YHR169W.
GeneID856574.
KEGGsce:YHR169W.

Organism-specific databases

CYGDYHR169w.
SGDS000001212. DBP8.

Phylogenomic databases

eggNOGCOG0513.
GeneTreeENSGT00700000105515.
HOGENOMHOG000268802.
KOK14778.
OMAFRNLCAI.
OrthoDBEOG4PP1RW.

Enzyme and pathway databases

BioCycYEAST:G3O-31203-MONOMER.

Gene expression databases

GenevestigatorP38719.
GermOnlineYHR169W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982426.

Entry information

Entry nameDBP8_YEAST
AccessionPrimary (citable) accession number: P38719
Secondary accession number(s): D3DLB8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 29, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

SIMILARITY comments

Index of protein domains and families