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Protein

ATP-dependent RNA helicase DHH1

Gene

DHH1

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 involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1 (PubMed:11780629, PubMed:12032091, PubMed:11696541, PubMed:12730603, PubMed:15703442. PubMed:15706350). Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs (PubMed:15166134). May also have a role in translation and mRNA nuclear export (PubMed:12930949). Required for sporulation (PubMed:12930949). Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 (PubMed:26098573).9 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi90 – 97ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • chromatin binding Source: SGD
  • mRNA binding Source: SGD
  • translation regulator activity, nucleic acid binding Source: SGD

GO - Biological processi

  • cytoplasmic mRNA processing body assembly Source: SGD
  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  • mRNA processing Source: UniProtKB-KW
  • mRNA transport Source: UniProtKB-KW
  • negative regulation of translation Source: SGD
  • negative regulation of translational elongation Source: SGD
  • RNA secondary structure unwinding Source: GO_Central
  • stress granule assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA transport, Translation regulation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29554-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DHH1Curated (EC:3.6.4.13Curated)
Alternative name(s):
DExD/H-box helicase 11 Publication
Gene namesi
Name:DHH11 Publication
Ordered Locus Names:YDL160CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL160C.
SGDiS000002319. DHH1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • cytoplasmic side of membrane Source: SGD
  • cytoplasmic stress granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Leads to an increased in autophagy flux (PubMed:26098573). Causes an accumulation of ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 transcripts in nutrient-replete conditions (PubMed:26098573).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi89R → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius; when associated with A-91. Impairs RNA binding in vitro. 1 Publication1
Mutagenesisi91K → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius; when associated with A-89. Impairs RNA binding in vitro. 1 Publication1
Mutagenesisi195D → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. 1 Publication1
Mutagenesisi196E → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. 1 Publication1
Mutagenesisi345R → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. 1 Publication1
Mutagenesisi346G → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. 1 Publication1
Mutagenesisi369H → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. 1 Publication1
Mutagenesisi370R → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000550441 – 506ATP-dependent RNA helicase DHH1Add BLAST506

Proteomic databases

MaxQBiP39517.
PRIDEiP39517.

PTM databases

iPTMnetiP39517.

Interactioni

Subunit structurei

Associated with the CCR4-NOT complex and possibly other big complexes (PubMed:9504907, PubMed:12930949). Interacts with CDC39/NOT1 (PubMed:11696541). Interacts with DCP1, LSM1, and POP2 (PubMed:9504907, PubMed:11780629). Interacts with IGO1 (PubMed:20471941). Interacts with PAT1 and with KEM1, the major 5'-3' exonuclease (PubMed:11780629, PubMed:12032091).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EDC3P399983EBI-158,EBI-22300
LSM1P470173EBI-158,EBI-174
LSM4P400703EBI-158,EBI-188
LSM7P539053EBI-158,EBI-141
PAT1P256444EBI-158,EBI-204
POP2P390083EBI-158,EBI-13629

Protein-protein interaction databases

BioGridi31903. 394 interactors.
DIPiDIP-1243N.
IntActiP39517. 38 interactors.
MINTiMINT-385061.

Structurei

Secondary structure

1506
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi48 – 51Combined sources4
Helixi55 – 63Combined sources9
Helixi71 – 82Combined sources12
Beta strandi86 – 89Combined sources4
Helixi96 – 107Combined sources12
Beta strandi117 – 120Combined sources4
Helixi124 – 137Combined sources14
Turni138 – 142Combined sources5
Beta strandi145 – 148Combined sources4
Beta strandi150 – 152Combined sources3
Helixi154 – 160Combined sources7
Beta strandi166 – 170Combined sources5
Helixi172 – 180Combined sources9
Beta strandi191 – 196Combined sources6
Helixi197 – 200Combined sources4
Helixi203 – 213Combined sources11
Beta strandi221 – 227Combined sources7
Helixi231 – 240Combined sources10
Beta strandi245 – 248Combined sources4
Beta strandi258 – 264Combined sources7
Helixi267 – 269Combined sources3
Helixi270 – 280Combined sources11
Beta strandi284 – 289Combined sources6
Helixi293 – 306Combined sources14
Beta strandi310 – 313Combined sources4
Helixi319 – 330Combined sources12
Beta strandi333 – 341Combined sources9
Beta strandi343 – 346Combined sources4
Beta strandi352 – 359Combined sources8
Helixi364 – 371Combined sources8
Beta strandi373 – 375Combined sources3
Beta strandi381 – 387Combined sources7
Helixi389 – 391Combined sources3
Helixi392 – 402Combined sources11
Beta strandi406 – 408Combined sources3
Helixi415 – 417Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S2MX-ray2.10A31-425[»]
4BRUX-ray3.24A46-422[»]
4BRWX-ray2.80A46-422[»]
ProteinModelPortaliP39517.
SMRiP39517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 247Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini257 – 417Helicase C-terminalPROSITE-ProRule annotationAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi46 – 74Q motifAdd BLAST29
Motifi195 – 198DEAD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi434 – 505Gln-richAdd BLAST72

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

GeneTreeiENSGT00860000133781.
HOGENOMiHOG000268797.
InParanoidiP39517.
KOiK12614.
OMAiLQEPVHI.
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.

P39517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSINNNFNT NNNSNTDLDR DWKTALNIPK KDTRPQTDDV LNTKGNTFED
60 70 80 90 100
FYLKRELLMG IFEAGFEKPS PIQEEAIPVA ITGRDILARA KNGTGKTAAF
110 120 130 140 150
VIPTLEKVKP KLNKIQALIM VPTRELALQT SQVVRTLGKH CGISCMVTTG
160 170 180 190 200
GTNLRDDILR LNETVHILVG TPGRVLDLAS RKVADLSDCS LFIMDEADKM
210 220 230 240 250
LSRDFKTIIE QILSFLPPTH QSLLFSATFP LTVKEFMVKH LHKPYEINLM
260 270 280 290 300
EELTLKGITQ YYAFVEERQK LHCLNTLFSK LQINQAIIFC NSTNRVELLA
310 320 330 340 350
KKITDLGYSC YYSHARMKQQ ERNKVFHEFR QGKVRTLVCS DLLTRGIDIQ
360 370 380 390 400
AVNVVINFDF PKTAETYLHR IGRSGRFGHL GLAINLINWN DRFNLYKIEQ
410 420 430 440 450
ELGTEIAAIP ATIDKSLYVA ENDETVPVPF PIEQQSYHQQ AIPQQQLPSQ
460 470 480 490 500
QQFAIPPQQH HPQFMVPPSH QQQQAYPPPQ MPSQQGYPPQ QEHFMAMPPG

QSQPQY
Length:506
Mass (Da):57,544
Last modified:February 1, 1995 - v1
Checksum:i062CFA56DF6F2CEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66057 Genomic DNA. Translation: CAA46853.1.
Z67750 Genomic DNA. Translation: CAA91586.1.
Z74208 Genomic DNA. Translation: CAA98734.1.
BK006938 Genomic DNA. Translation: DAA11700.1.
PIRiS31229.
RefSeqiNP_010121.1. NM_001180220.1.

Genome annotation databases

EnsemblFungiiYDL160C; YDL160C; YDL160C.
GeneIDi851394.
KEGGisce:YDL160C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66057 Genomic DNA. Translation: CAA46853.1.
Z67750 Genomic DNA. Translation: CAA91586.1.
Z74208 Genomic DNA. Translation: CAA98734.1.
BK006938 Genomic DNA. Translation: DAA11700.1.
PIRiS31229.
RefSeqiNP_010121.1. NM_001180220.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S2MX-ray2.10A31-425[»]
4BRUX-ray3.24A46-422[»]
4BRWX-ray2.80A46-422[»]
ProteinModelPortaliP39517.
SMRiP39517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31903. 394 interactors.
DIPiDIP-1243N.
IntActiP39517. 38 interactors.
MINTiMINT-385061.

PTM databases

iPTMnetiP39517.

Proteomic databases

MaxQBiP39517.
PRIDEiP39517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL160C; YDL160C; YDL160C.
GeneIDi851394.
KEGGisce:YDL160C.

Organism-specific databases

EuPathDBiFungiDB:YDL160C.
SGDiS000002319. DHH1.

Phylogenomic databases

GeneTreeiENSGT00860000133781.
HOGENOMiHOG000268797.
InParanoidiP39517.
KOiK12614.
OMAiLQEPVHI.
OrthoDBiEOG092C2B1L.

Enzyme and pathway databases

BioCyciYEAST:G3O-29554-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39517.
PROiP39517.

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 nameiDHH1_YEAST
AccessioniPrimary (citable) accession number: P39517
Secondary accession number(s): D6VRJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 42900 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.