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Protein

ATP-dependent RNA helicase DBP5

Gene

DBP5

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

Functioni

ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription.11 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi138 – 1458ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • RNA binding Source: UniProtKB-KW
  • RNA-dependent ATPase activity Source: SGD
  • RNA helicase activity Source: SGD

GO - Biological processi

  • mRNA export from nucleus Source: SGD
  • protein transport Source: UniProtKB-KW
  • RNA secondary structure unwinding Source: GO_Central
  • translational termination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DBP5 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 5
Helicase CA5/6
Ribonucleic acid-trafficking protein 8
Gene namesi
Name:DBP5
Synonyms:RAT8
Ordered Locus Names:YOR046C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR046C.
SGDiS000005572. DBP5.

Subcellular locationi

GO - Cellular componenti

  • cellular bud tip Source: SGD
  • cytoplasm Source: SGD
  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore cytoplasmic filaments Source: SGD
  • nucleus Source: SGD
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701P → H in RAT8-7; accumulates poly(A)+ RNA in the nucleus at 16 degrees Celsius. 1 Publication
Mutagenesisi171 – 1711S → P in DBP5-2; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with L-236 and F-245. 1 Publication
Mutagenesisi220 – 2201L → P in DBP5-1; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with S-466. 1 Publication
Mutagenesisi236 – 2361F → L in DBP5-2; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with P-171 and F-245. 1 Publication
Mutagenesisi267 – 2671L → P in RAT8-2; accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. 1 Publication
Mutagenesisi345 – 3451V → F in DBP5-2; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with P-171 and L-236. 1 Publication
Mutagenesisi385 – 3851I → D in RAT8-3; accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. 1 Publication
Mutagenesisi466 – 4661T → S in DBP5-1; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with P-220. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482ATP-dependent RNA helicase DBP5PRO_0000055019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei162 – 1621PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20449.

PTM databases

iPTMnetiP20449.

Interactioni

Subunit structurei

Associates with the nuclear pore complex. Interacts with NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary for the association to the nuclear pore complex. Interacts also with the TFIIH complex subunits TFB1, TFB2 and RAD3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GFD1Q048392EBI-5617,EBI-27549
ZDS1P501113EBI-5617,EBI-29626

Protein-protein interaction databases

BioGridi34447. 182 interactions.
DIPiDIP-2352N.
IntActiP20449. 7 interactions.
MINTiMINT-488024.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi78 – 803Combined sources
Helixi83 – 853Combined sources
Helixi87 – 904Combined sources
Helixi94 – 974Combined sources
Helixi101 – 1099Combined sources
Beta strandi110 – 1134Combined sources
Helixi117 – 12711Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi134 – 1374Combined sources
Helixi144 – 15512Combined sources
Beta strandi165 – 1684Combined sources
Helixi172 – 18514Combined sources
Turni186 – 1883Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi210 – 2145Combined sources
Helixi216 – 2249Combined sources
Beta strandi235 – 2395Combined sources
Helixi241 – 2466Combined sources
Helixi250 – 25910Combined sources
Turni261 – 2644Combined sources
Beta strandi266 – 2727Combined sources
Helixi276 – 28510Combined sources
Beta strandi290 – 2923Combined sources
Helixi296 – 2983Combined sources
Turni301 – 3033Combined sources
Beta strandi304 – 3107Combined sources
Helixi314 – 32512Combined sources
Turni326 – 3294Combined sources
Beta strandi330 – 3367Combined sources
Helixi340 – 35213Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi362 – 3643Combined sources
Helixi366 – 37712Combined sources
Turni378 – 3803Combined sources
Beta strandi383 – 3864Combined sources
Helixi388 – 3903Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi399 – 4068Combined sources
Beta strandi413 – 4153Combined sources
Helixi417 – 4248Combined sources
Helixi425 – 4273Combined sources
Beta strandi434 – 4407Combined sources
Helixi443 – 45513Combined sources
Turni456 – 4583Combined sources
Beta strandi462 – 4654Combined sources
Helixi469 – 48012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KBENMR-A71-296[»]
2KBFNMR-A296-482[»]
3GFPX-ray1.80A296-482[»]
3PEUX-ray2.60A297-482[»]
3PEVX-ray2.50A297-482[»]
3PEWX-ray1.50A91-482[»]
3PEYX-ray1.40A91-482[»]
3RRMX-ray2.88A91-482[»]
3RRNX-ray4.00A91-482[»]
5ELXX-ray1.81A91-481[»]
ProteinModelPortaliP20449.
SMRiP20449. Positions 80-481.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20449.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 292168Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini303 – 480178Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi92 – 12029Q motifAdd
BLAST
Motifi239 – 2424DEAD 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

GeneTreeiENSGT00530000063236.
HOGENOMiHOG000268797.
InParanoidiP20449.
KOiK18655.
OMAiFAPQANE.
OrthoDBiEOG092C2B1L.

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.

P20449-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDTKRDPAD LLASLKIDNE KEDTSEVSTK ETVKSQPEKT ADSIKPAEKL
60 70 80 90 100
VPKVEEKKTK QEDSNLISSE YEVKVKLADI QADPNSPLYS AKSFDELGLA
110 120 130 140 150
PELLKGIYAM KFQKPSKIQE RALPLLLHNP PRNMIAQSQS GTGKTAAFSL
160 170 180 190 200
TMLTRVNPED ASPQAICLAP SRELARQTLE VVQEMGKFTK ITSQLIVPDS
210 220 230 240 250
FEKNKQINAQ VIVGTPGTVL DLMRRKLMQL QKIKIFVLDE ADNMLDQQGL
260 270 280 290 300
GDQCIRVKRF LPKDTQLVLF SATFADAVRQ YAKKIVPNAN TLELQTNEVN
310 320 330 340 350
VDAIKQLYMD CKNEADKFDV LTELYGLMTI GSSIIFVATK KTANVLYGKL
360 370 380 390 400
KSEGHEVSIL HGDLQTQERD RLIDDFREGR SKVLITTNVL ARGIDIPTVS
410 420 430 440 450
MVVNYDLPTL ANGQADPATY IHRIGRTGRF GRKGVAISFV HDKNSFNILS
460 470 480
AIQKYFGDIE MTRVPTDDWD EVEKIVKKVL KD
Length:482
Mass (Da):53,874
Last modified:October 1, 1996 - v2
Checksum:iC50CAFE8C060D46B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28135 Genomic DNA. Translation: AAB01679.1.
Z74954 Genomic DNA. Translation: CAA99237.1.
Z74955 Genomic DNA. Translation: CAA99239.1.
BK006948 Genomic DNA. Translation: DAA10828.1.
PIRiS66920.
RefSeqiNP_014689.1. NM_001183465.1.

Genome annotation databases

EnsemblFungiiYOR046C; YOR046C; YOR046C.
GeneIDi854211.
KEGGisce:YOR046C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28135 Genomic DNA. Translation: AAB01679.1.
Z74954 Genomic DNA. Translation: CAA99237.1.
Z74955 Genomic DNA. Translation: CAA99239.1.
BK006948 Genomic DNA. Translation: DAA10828.1.
PIRiS66920.
RefSeqiNP_014689.1. NM_001183465.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KBENMR-A71-296[»]
2KBFNMR-A296-482[»]
3GFPX-ray1.80A296-482[»]
3PEUX-ray2.60A297-482[»]
3PEVX-ray2.50A297-482[»]
3PEWX-ray1.50A91-482[»]
3PEYX-ray1.40A91-482[»]
3RRMX-ray2.88A91-482[»]
3RRNX-ray4.00A91-482[»]
5ELXX-ray1.81A91-481[»]
ProteinModelPortaliP20449.
SMRiP20449. Positions 80-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34447. 182 interactions.
DIPiDIP-2352N.
IntActiP20449. 7 interactions.
MINTiMINT-488024.

PTM databases

iPTMnetiP20449.

Proteomic databases

MaxQBiP20449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR046C; YOR046C; YOR046C.
GeneIDi854211.
KEGGisce:YOR046C.

Organism-specific databases

EuPathDBiFungiDB:YOR046C.
SGDiS000005572. DBP5.

Phylogenomic databases

GeneTreeiENSGT00530000063236.
HOGENOMiHOG000268797.
InParanoidiP20449.
KOiK18655.
OMAiFAPQANE.
OrthoDBiEOG092C2B1L.

Enzyme and pathway databases

BioCyciYEAST:G3O-33590-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP20449.
PROiP20449.

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...

Entry informationi

Entry nameiDBP5_YEAST
AccessioniPrimary (citable) accession number: P20449
Secondary accession number(s): D6W2B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 170 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 14900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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