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Protein

ATP-dependent RNA helicase DBP1

Gene

DBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Redundant to DED1, may be required in conditions in which DED1 expression is decreased.By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi198 – 2058ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • chromosome segregation Source: GO_Central
  • regulation of gene expression Source: GO_Central
  • RNA secondary structure unwinding Source: GO_Central
  • translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34018-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DBP1 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 1
Helicase CA1
Gene namesi
Name:DBP1
Ordered Locus Names:YPL119C
ORF Names:LPH8C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL119C.
SGDiS000006040. DBP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic ribonucleoprotein granule Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617ATP-dependent RNA helicase DBP1PRO_0000055016Add
BLAST

Proteomic databases

MaxQBiP24784.

Interactioni

Protein-protein interaction databases

BioGridi36062. 41 interactions.
DIPiDIP-2576N.
IntActiP24784. 9 interactions.
MINTiMINT-426870.

Structurei

3D structure databases

ProteinModelPortaliP24784.
SMRiP24784. Positions 107-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini185 – 374190Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini385 – 545161Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi154 – 18229Q motifAdd
BLAST
Motifi318 – 3214DEAD box

Domaini

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

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00770000120531.
HOGENOMiHOG000268804.
InParanoidiP24784.
KOiK11594.
OMAiENGVHGK.
OrthoDBiEOG7TJ3T2.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLPQKVSN LSINNKENGG GGGKSSYVPP HLRSRGKPSF ERSTPKQEDK
60 70 80 90 100
VTGGDFFRRA GRQTGNNGGF FGFSKERNGG TSANYNRGGS SNYKSSGNRW
110 120 130 140 150
VNGKHIPGPK NAKLEAELFG VHDDPDYHSS GIKFDNYDNI PVDASGKDVP
160 170 180 190 200
EPILDFSSPP LDELLMENIK LASFTKPTPV QKYSIPIVTK GRDLMACAQT
210 220 230 240 250
GSGKTGGFLF PLFTELFRSG PSPVPEKAQS FYSRKGYPSA LVLAPTRELA
260 270 280 290 300
TQIFEEARKF TYRSWVRPCV VYGGAPIGNQ MREVDRGCDL LVATPGRLND
310 320 330 340 350
LLERGKVSLA NIKYLVLDEA DRMLDMGFEP QIRHIVEECD MPSVENRQTL
360 370 380 390 400
MFSATFPVDI QHLARDFLDN YIFLSVGRVG STSENITQRI LYVDDMDKKS
410 420 430 440 450
ALLDLLSAEH KGLTLIFVET KRMADQLTDF LIMQNFKATA IHGDRTQAER
460 470 480 490 500
ERALSAFKAN VADILVATAV AARGLDIPNV THVINYDLPS DIDDYVHRIG
510 520 530 540 550
RTGRAGNTGV ATSFFNSNNQ NIVKGLMEIL NEANQEVPTF LSDLSRQNSR
560 570 580 590 600
GGRTRGGGGF FNSRNNGSRD YRKHGGNGSF GSTRPRNTGT SNWGSIGGGF
610
RNDNEKNGYG NSNASWW
Length:617
Mass (Da):67,917
Last modified:October 1, 1996 - v2
Checksum:i8152404B7628671D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 442ST → RS in CAA39465 (PubMed:1857205).Curated
Sequence conflicti48 – 481E → K in CAA39465 (PubMed:1857205).Curated
Sequence conflicti88 – 881G → R in CAA39465 (PubMed:1857205).Curated
Sequence conflicti115 – 1151E → QK in CAA39465 (PubMed:1857205).Curated
Sequence conflicti496 – 4961V → I no nucleotide entry (PubMed:2406722).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55993 Genomic DNA. Translation: CAA39465.1.
U43503 Genomic DNA. Translation: AAB68243.1.
BK006949 Genomic DNA. Translation: DAA11315.1.
PIRiS62003.
RefSeqiNP_015206.1. NM_001183933.1.

Genome annotation databases

EnsemblFungiiYPL119C; YPL119C; YPL119C.
GeneIDi855984.
KEGGisce:YPL119C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55993 Genomic DNA. Translation: CAA39465.1.
U43503 Genomic DNA. Translation: AAB68243.1.
BK006949 Genomic DNA. Translation: DAA11315.1.
PIRiS62003.
RefSeqiNP_015206.1. NM_001183933.1.

3D structure databases

ProteinModelPortaliP24784.
SMRiP24784. Positions 107-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36062. 41 interactions.
DIPiDIP-2576N.
IntActiP24784. 9 interactions.
MINTiMINT-426870.

Proteomic databases

MaxQBiP24784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL119C; YPL119C; YPL119C.
GeneIDi855984.
KEGGisce:YPL119C.

Organism-specific databases

EuPathDBiFungiDB:YPL119C.
SGDiS000006040. DBP1.

Phylogenomic databases

GeneTreeiENSGT00770000120531.
HOGENOMiHOG000268804.
InParanoidiP24784.
KOiK11594.
OMAiENGVHGK.
OrthoDBiEOG7TJ3T2.

Enzyme and pathway databases

BioCyciYEAST:G3O-34018-MONOMER.

Miscellaneous databases

PROiP24784.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A suppressor of yeast spp81/ded1 mutations encodes a very similar putative ATP-dependent RNA helicase."
    Jamieson D.J., Beggs J.D.
    Mol. Microbiol. 5:805-812(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: DBY939.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Identification of five putative yeast RNA helicase genes."
    Chang T.-H., Arenas J., Abelson J.
    Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 316-500.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Dynamics and processivity of 40S ribosome scanning on mRNA in yeast."
    Berthelot K., Muldoon M., Rajkowitsch L., Hughes J., McCarthy J.E.G.
    Mol. Microbiol. 51:987-1001(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiDBP1_YEAST
AccessioniPrimary (citable) accession number: P24784
Secondary accession number(s): D6W3P9, P20446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1480 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.