Information on EC 3.6.4.13 - RNA helicase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Yellow fever virus

EC NUMBER
COMMENTARY
3.6.4.13
-
RECOMMENDED NAME
GeneOntology No.
RNA helicase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a nucleoside triphosphate + H2O = a nucleoside diphosphate + phosphate
show the reaction diagram
-
-
-
-
a nucleoside triphosphate + H2O = a nucleoside diphosphate + phosphate
show the reaction diagram
catalytic mechanism involving a bound sulfate ion, NTPase active site structure, nucleic acid binding site
-
ATP + H2O = ADP + phosphate
show the reaction diagram
-
-
-
-
ATP + H2O = ADP + phosphate
show the reaction diagram
models: DbpA functions as an active monomer that possesses two distinct RNA binding sites, one in the helicase core domain and the other in the carboxyl-terminal domain that recognizes 23 S rRNA and interacts specifically with hairpin 92 of the peptidyl transferase center
-
ATP + H2O = ADP + phosphate
show the reaction diagram
quantitative kinetic and equilibrium characterization of the rRNA-activated ATPase cycle mechanism of DbpA
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (RNA helix unwinding)
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3' to 5' polarity [3], other show 5' to 3' polarity [8]. Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC 3.6.4.12 (DNA helicase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1a NTPase/helicase
-
-
ATP/dATP-dependent RNA helicase
-, EF409381
-
ATPase
-
-
ATPase/helicase
-
-
ATPase/helicase
Dengue virus PL046
-
-
-
ATPase/RNA helicase
-, EF409381
-
BmL3-helicase
-, EF409381
-
BMV 1a protein
-
-
Brr2p
-
-
Cbu_0670
Q83DM8
-
CrhR
Synechocystis sp. PCC6803
-
-
-
DBP2
O60231
-
DDX17
Q501J6
-
DDX19
Q9UMR2
-
DDX25
Q9UHL0
-
DDX25
Q9QY15
-
DDX25
Q9QY16
-
DDX3
-
-
DDX3
O00571
-
DDX3X
O00571
the gene is localized to the X chromosome
DDX3Y
O15523
the gene is localized to the Y chromosome
DDX4
Q9NQI0
-
DDX5
P17844
-
DDX5
Q61656
-
DEAD box helicase
-
-
DEAD box RNA helicase
-
-
DEAD box RNA helicase
-
-
DEAD box RNA helicase
-
-
DEAD-box protein DED1
P06634
-
DEAD-box RNA helicase
-
-
DEAD-box RNA helicase
-
-
DEAD-box RNA helicase
P06634
-
DEAD-box RNA helicase
B9VSG1
-
DEAD-box RNA helicase
-
-
DEAD-box RNA helicase
Q7ZX48
-
DEAD-box rRNA helicase
-
-
DEAH-box protein 2
O60231
-
DEAH-box RNA helicase
O60231
-
DENV NS3H
-
-
DENV NS3H
Dengue virus PL046
-
-
-
DEx(H/D)RNA helicase
-
-
DEXD/H-box RNA helicase
Q9UMR2
-
DExH protein RNA helicase A
-
-
DHX36
-
-
DHX9
Q08211
-
Dhx9/RNA helicase A
-
-
EhDEAD1 RNA helicase
-
-
eIF4A
P29562
-
eIF4A helicase
P29562
-
eIF4AIII
P38919
-
eukaryotic initiation factor eIF 4A
P29562
-
FRH
Neurospora sp.
-
-
FRQ-interacting RNA helicase
Neurospora sp.
-
-
gonadotropin-regulated testicular RNA helicase
-
-
GRTH
-
-
GRTH/DDX25
Q9UHL0
-
GRTH/DDX25
-
-
HCV NS3 helicase
-
-
helicase
-
-
helicase
Dengue virus PL046
-
-
-
helicase B
-
-
helicase/nucleoside triphosphatase
-
-
KOKV helicase
-
-
non structural protein 3
-
ambiguous
non-structural 3
-
-
non-structural protein 3
-
-
non-structural protein 3 protein
-
-
non-structural protein 3 protein
Rice hoja blanca virus RHBV
-
-
-
nonstructural protein 3
Q9YS30
-
nonstructural protein 3
Classical swine fever virus CSFV
Q9YS30
-
-
nonstructural protein 3
-
-
nonstructural protein 3
-
-
nonstructural protein 3
-
; ambiguous
nonstructural protein 3
-
ambiguous
nonstructural protein 3
Q9WPH5
ambiguous
nonstructural protein 3
P27395
ambiguous
nonstructural protein 3
-
ambiguous
NS3
Classical swine fever virus CSFV
Q9YS30
-
-
NS3
-
ambiguous
NS3
Q9WPH5
ambiguous
NS3
West Nile virus WNV
-
-
-
NS3 ATPase/helicase
-
-
NS3 ATPase/helicase
Dengue virus PL046
-
-
-
NS3 helicase
-
-
NS3 helicase
-
-
NS3 helicase
-
-
NS3 NTPase/helicase
-
; ambiguous
NS3 NTPase/helicase
West Nile virus WNV
-
; ambiguous
-
NS3 protein
-
-
NS3 protein
Dengue virus PL046
-
-
-
NS3 protein
-
ambiguous
NS3 protein
-
-
NS3 protein
Rice hoja blanca virus RHBV
-
-
-
NS3 protein
-
-
NTPase/helicase
-
-
NTPase/helicase
-
ambiguous
nucleoside 5'-triphosphatase
-
-
nucleoside triphosphatase/helicase
-
-
nucleoside triphosphatase/RNA helicase and 5'-RNA triphosphatase
-
-
p54 RNA helicase
P26196
-
p68 RNA helicase
-
-
p68 RNA helicase
-
-
protein NS3
-
ambiguous
RNA DEAD-box helicase
Q83DM8
-
RNA helicase
-
-
RNA helicase A
-
-
RNA helicase A
Q08211
-
RNA helicase CrhR
-
-
RNA helicase DDX3
O00571
-
RNA helicase Ddx39
Q7ZX48
-
RNA helicase Hera
-
-
RNA Helicase p68
P17844
-
RNA helicase RHAU
-
-
RNA-dependent ATPase
P38919
-
RNA-dependent NTPase/helicase
-
-
RTPase
-
-
slr0083
-
gene name
SpolvlgA
B9VSG1
-
Supv3L1
Q80YD1
-
TGBp1 NTPase/helicase domain
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
i.e. BMV
-
-
Manually annotated by BRENDA team
-
EF409381
GenBank
Manually annotated by BRENDA team
Classical swine fever virus CSFV
CSFV
SwissProt
Manually annotated by BRENDA team
; serotype 2, PL046 strain
-
-
Manually annotated by BRENDA team
; serotype 4
-
-
Manually annotated by BRENDA team
i.e. DNV
-
-
Manually annotated by BRENDA team
i.e. DEN2
-
-
Manually annotated by BRENDA team
Dengue virus PL046
serotype 2, PL046 strain
-
-
Manually annotated by BRENDA team
i.e. HCV
-
-
Manually annotated by BRENDA team
recombinant HCV helicase constructs, nonstructural protein 3
-
-
Manually annotated by BRENDA team
subtype 1b
SwissProt
Manually annotated by BRENDA team
viral genotype 1a, version H77
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
transgenic
-
-
Manually annotated by BRENDA team
Neurospora sp.
-
-
-
Manually annotated by BRENDA team
Rice hoja blanca virus RHBV
RHBV
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
-
-
-
Manually annotated by BRENDA team
West Nile virus WNV
WNV
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
knockdown of endogenous RHA significantly reduces the interaction of RNA polymerase II with beta-actin
malfunction
-
mutation of the crhR gene by replacement with a spectinomycin-resistance gene cassette. The resultant DELTAcrhR mutant exhibits a phenotype of slow growth at low temperatures. CrhR regulates the low-temperature-inducible expression of the heat-shock proteins groEL1 and groEL2, which, in turn, may be essential for acclimatization of Synechocystis cells to low temperatures
malfunction
Q80YD1
conditional ablation of Supv3L1 in adult mice leads to premature aging phenotypes including loss of muscle mass and adipose tissue and severe skin abnormalities
malfunction
-
wild type Synechocystis cells acclimatize to low temperature by energy redistribution (state transitions) and regulating the PSI and PSII stoichiometry. In contrast the mutant cells deficient in CrhR fail to operate state transitions and are unable to regulate the photosystem stoichiometry. Mutant cells deficient in CrhR can not acclimatize to low temperature
malfunction
-
when Vasa accumulation is attenuated by injection of Vasa morpholino antisense oligonucleotide in the early embryo, the cells show a severe delay in their cell cycle progression in a dose-dependent manner and lack normal spindles even following chromosome condensation
malfunction
-
by using wild-type, helps mutant and overexpression lines of Arabidopsis, it is shown that, in the low-K+ condition, AtHELPS inhibits Arabidopsis seed germination via decreased K+ influx into roots. Expression of AKT1, CBL1, CBL9 and CIPK23 is regulated by AtHELPS under low-K+ stress
malfunction
-
DDX3 knockdown blocks the shuttling of DDX5 to the nucleus
malfunction
-
crhR deletion results in failure to cold acclimate: there is reduced growth at 24C and marked impairment of growth at 20C compared to wild-type. Using a proteomic approach differentially expressed proteins are identified
malfunction
-
RHAU knockdown by small interfering RNA (siRNA) results in a significant reduction in average telomere lengths supporting an impact of RHAU on telomerase function
malfunction
-
knockdown of RH22 expression results in virescent seedlings with clear defects in chloroplast ribosomal RNA accumulation. The precursors of 23S and 4.5S, but not 16S, rRNA accumulate in rh22 mutants
malfunction
-
disruption of the hrpA gene results in a complete loss in the ability of the spirochetes to infect mice by needle inoculation. Protein expression analysis show a total of 187 differentially regulated proteins in an hrpA background: 90 downregulated and 97 upregulated. 42 of the 90 downregulated and 65 of the 97 upregulated proteins are not regulated under any conditions by the previously reported regulators in Borrelia burgdorferi (bosR, rrp2, rpoN, rpoS or rrp1)
malfunction
-
knockdown of RHA prevents formation of polysomes on collagen mRNAs and dramatically reduces synthesis of collagen protein, without affecting the level of the mRNAs
malfunction
Synechocystis sp. PCC6803
-
crhR deletion results in failure to cold acclimate: there is reduced growth at 24C and marked impairment of growth at 20C compared to wild-type. Using a proteomic approach differentially expressed proteins are identified
-
metabolism
-
UV cross-linking experiments show that both RNA helicase proteins are involved in mRNP metabolism and that DDX3 affects the shuttling of DDX5 to the nucleus; UV cross-linking experiments show that both RNA helicase proteins are involved in mRNP metabolism and that DDX3 affects the shuttling of DDX5 to the nucleus
physiological function
-
the enzyme functions under cold stress conditions
physiological function
-
the enzyme plays an important role in linking beta-actin with RNA polymerase II and functions in gene transcription regulation
physiological function
-
the enzyme plays an essential role in pre-mRNA splicing. Mutation within hBrr2p can be linked to autosomal dominant retinitis pigmentosa
physiological function
-
through its export/transport function as a component of mRNP (mRNAs that associate with ribonuclear particles) GRTH is essential to govern the structure of the chromatoid body in spermatids and to maintain systems that may participate in mRNA storage and their processing during spermatogenesis
physiological function
-
the protein plays a very important role in early organ development and maturation, function of the protein in transcriptional regulation and pre-mRNA splicing
physiological function
Q7ZX48
is a part of the homeostatic machinery that regulates the switch between cellular proliferation and differentiation
physiological function
P26196
ATPase/helicase activity allows protein complex remodeling that dictates the balance between repressors and an activator of translation
physiological function
-
translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
physiological function
-
the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
physiological function
-
phosphorylation of p68 RNA helicase at Y593 upregulates transcription of the Snail1 gene. The phosphorylated p68 activates transcription of the Snail1 gene by promoting histone deacetylase dissociation from the Snail1 promoter. p68 interacts with the nuclear remodeling and deacetylation complex MBD3:Mi-2/NuRD. The DEAD-box RNA unwindase could potentially regulate gene expression by functioning as a protein displacer to modulate proteinprotein interactions at the chromatin-remodeling complex
physiological function
Q80YD1
plays a critical role in the mitochondrial RNA surveillance and degradation machinery
physiological function
-, Q83DM8
in vitro efficiency of L1917 intron splicing is significantly enhanced in the presence of a recombinant Coxiella RNA DEAD-box helicase relative to that of controls, suggesting that this enzyme may serve as an intron RNA splice facilitator in vivo
physiological function
-
using an RNA affinity pulldown-coupled mass spectrometry approach DDX5/RNA helicase p68 is identified as an activator of tau exon 10 splicing. p68 regulates tau exon 10 splicing by interacting with the stem-loop region, destabilizing the stem structure, and facilitating U1snRNP binding to this 5' splice site
physiological function
-
RH22 may function in the assembly of 50S ribosomal subunits in chloroplasts
physiological function
-
RHA interacts with LARP6, which recruits RHA to the 5' UTR of collagen mRNAs. There, RHA activity is necessary for efficient formation of polysomes and a high level of collagen protein synthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-dideoxy-ATP + H2O
2',3'-dideoxy-ADP + phosphate
show the reaction diagram
-
53% of the phosphohydrolase activity with ATP
-
-
?
2',3'-dideoxy-GTP + H2O
2',3'-dideoxy-GDP + phosphate
show the reaction diagram
-
28% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate
show the reaction diagram
-
62% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-GTP + H2O
2'-deoxy-GDP + phosphate
show the reaction diagram
-
39% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-L-GTP + H2O
2'-deoxy-L-GDP + phosphate
show the reaction diagram
-
11% of the phosphohydrolase activity with ATP
-
-
?
2'-fluoro-2'-deoxy-ATP + H2O
2'-fluoro-2'-deoxy-ADP + phosphate
show the reaction diagram
-
63% of the phosphohydrolase activity with ATP
-
-
?
2'-fluoro-2'-deoxy-GTP + H2O
2'-fluoro-2'-deoxy-GDP + phosphate
show the reaction diagram
-
22% of the phosphohydrolase activity with ATP
-
-
?
2'-O-methyl-GTP + H2O
2'-O-methyl-GDP + phosphate
show the reaction diagram
-
24% of the phosphohydrolase activity with ATP
-
-
?
2-amino-ATP + H2O
2-amino-ADP + phosphate
show the reaction diagram
-
103% of the phosphohydrolase activity with ATP
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-ADP + phosphate
show the reaction diagram
-
40% of the phosphohydrolase activity with ATP
-
-
?
3'-deoxy-ATP + H2O
3'-deoxy-ADP + phosphate
show the reaction diagram
-
60% of the phosphohydrolase activity with ATP
-
-
?
3'-deoxy-GTP + H2O
3'-deoxy-GDP + phosphate
show the reaction diagram
-
12% of the phosphohydrolase activity with ATP
-
-
?
3'-O-methyl-GTP + H2O
3'-O-methyl-GDP + phosphate
show the reaction diagram
-
35% of the phosphohydrolase activity with ATP
-
-
?
6-methyl-thio-GTP + H2O
6-methyl-thio-GDP + phosphate
show the reaction diagram
-
40% of the phosphohydrolase activity with ATP
-
-
?
6-methyl-thio-ITP + H2O
6-methyl-thio-IDP + phosphate
show the reaction diagram
-
16% of the phosphohydrolase activity with ATP
-
-
?
6-thio-GTP + H2O
6-thio-GDP + phosphate
show the reaction diagram
-
93% of the phosphohydrolase activity with ATP
-
-
?
7-methyl-GTP + H2O
7-methyl-GDP + phosphate
show the reaction diagram
-
14% of the phosphohydrolase activity with ATP
-
-
?
8-bromo-ATP + H2O
8-bromo-ADP + phosphate
show the reaction diagram
-
124% of the phosphohydrolase activity with ATP
-
-
?
8-bromo-GTP + H2O
8-bromo-GDP + phosphate
show the reaction diagram
-
19% of the phosphohydrolase activity with ATP
-
-
?
8-iodo-GTP + H2O
8-iodo-GDP + phosphate
show the reaction diagram
-
54% of the phosphohydrolase activity with ATP
-
-
?
Ara-ATP + H2O
Ara-ADP + phosphate
show the reaction diagram
-
18% of the phosphohydrolase activity with ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27958
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9WPH5
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9QY16
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O60231
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O00571
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O15523, Q9NQI0, Q9UHL0
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q501J6, Q61656, Q9QY15
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27395
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-, Q9YS30
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-, EF409381
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UMR2
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q08211
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
preferred substrate for NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes. GRTH has a negative role on its mRNA stability
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P47047
Mtr4p can unwind duplex RNA in the presence of ATP and a single-stranded RNA tail in the 3' to 5' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
phosphohydrolase and helicase activities of NPH-II are essential for virus replication
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RHA is a coactivator in STAT6-mediated transcription, and this function is dependent on its helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O15523, Q9NQI0, Q9UHL0
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q501J6, Q61656, Q9QY15
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9QY16
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q501J6, Q61656, Q9QY15
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O15523, Q9NQI0, Q9UHL0
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P06634
the DEAD-box protein DED1 has the ability to balance RNA unwinding with a profound strand annealing activity in a highly dynamic fashion
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P47047
ATP and dATP are the preferred nucleotide substrates. In the presence of ATP or dATP Mtr4p unwinds the duplex region of a partial duplex RNA substrate in the 3' to 5' direction. Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P29562
eIF4A may interact directly with double-stranded RNA, and recognition of helicase substrates occurs via chemical and/or structural features of the duplex. The initial rate and amplitude of duplex unwinding by eIF4A is dependent on the overall stability, rather than the length or sequence, of the duplex substrate. eIF4A helicase activity is minimally dependent on the length of the single-stranded region adjacent to the double-stranded region of the substrate. Interestingly, eIF4A is able to unwind blunt-ended duplexes. eIF4A helicase activity is also affected by substitution of 2'-OH (RNA) groups with 2'-H (DNA) or 2'-methoxyethyl groups
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-, EF409381
either ATP or dATP is required for the unwinding activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9M6R6, -
either ATP or dATP is required for the unwinding activity, VrRH1 catalyzes unwinding of a double-stranded RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity requires the substrates possessing a 3' un-base-paired region on the RNA template strand. The NS3h helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of the RNA substrates. CSFV NS3 helicase activity requires a longer 3'-end single-stranded overhang for efficient duplex unwinding and the directionality of NS3 helicase unwinding is 3' to 5' with respect to the template strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P06634
promotes RNA unwinding. The enzyme also catalyzes strand annealing. The balance between unwinding and annealing activities of DED1 depends on the RNA substrate. ADP also modulates the balance between RNA unwinding and strand annealing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
recombinant EhDEAD1 protein presents ATPase activity and is able to bind and unwind RNA in an ATPase-dependent manner
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RNA helicase A utilizes all hydrolyzable NTPs without preference. RNA helicase A unwinds dsRNA only in a 3' to 5' direction. The enzyme can only translocate on RNA possessing 3 single-stranded regions
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P38919
RNA-dependent ATPase, helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the 3' to 5' helicase activity of DbpA can use a 3' single-stranded loading site on either strand of the substrate helix
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P0C6X1
the enzyme has both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the protein binds RNA and DNA in a sequence specific manner. ATP hydrolysis is stimulated by some nucleic acid polymers much better than it is stimulated by others. The range is quite dramatic. Poly(G) RNA does not stimulate at any measurable level, and poly(U) RNA (or DNA) stimulates best (up to 50 fold). HCV helicase unwinds a DNA duplex more efficiently than an RNA duplex. ATP binds HCV helicase between two RecA-like domains, causing a conformational change that leads to a decrease in the affinity of the protein for nucleic acids. One strand of RNA binds in a second cleft formed perpendicular to the ATP-binding cleft and its binding leads to stimulation of ATP hydrolysis. RNA and/or ATP binding likely causes rotation of domain 2 of the enzyme relative to domains 1 and 3, and somehow this conformational change allows the protein to move like a motor
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the Q motif regulates ATP binding and hydrolysis, the affinity of the protein for RNA substrates and the helicase activity. At least three different protein conformations that are associated with free, ADP-bound and ATP-bound forms of the protein
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
unwinds duplex RNA exclusively in a 3' to 5' direction with respect to the strand to which the enzyme is bound and along which it is presumed to translocate. NTP hydrolysis by RNA bound NPH-II1 drives processive translocation of the protein in a 3 to 5 direction along the RNA strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P26663
unwinds RNA in a discontinuous manner, pausing after long apparent steps of unwinding. It is proposed that the large kinetic step size of NS3 unwinding reflects a delayed, periodic release of the separated RNA product strand from a secondary binding site that is located in the NTPase domain (domain II) of NS3
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
NTPase activity analyzed, ambiguous helicase activity, enzyme capable for unwinding RNA and DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9WPH5
RNA-stimulated ATPase activities determined, interaction between the replicative component nonstructural protein 3 (NS3) with the nonstructural protein 4A (NS4A)
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27958
the Arg-rich amino acid motif HCV1487-1500, a fragment of domain 2 NS3 of Hepatitis C virus, as well as the complete domain 2, and domain 2 lacking the flexible loop localized between Val1458 and Thr1476, mediate competitive inhibition of diverse protein kinase C functions, inhibition of rat brain PKC, overview
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATPase activity, ATP binding mode, the ATP binding site is housed between these two subdomains. In the ATP binding pocket, a Mg ion is coordinated in a octahedral manner by the beta- and gamma-phosphate oxygen atoms from ATP, two equatorial water molecules and oxygen atoms from residues Glu285 in motif II, and Thr200 in motif I, overview
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
cooperative binding of ATP and RNA leads to a compact helicase structure
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27395
genome structure, crystals and three-dimensional structure determined, structure of NTP-binding region, conserved residues within the NTP-binding pocket, ATPase and RNA helicase activities determined
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
NS3 C-terminal domain catalyzes ATP hydrolysis in the presence of MgCl2 or MnCl2. MgCl2 is more effective than MnCl2 at inducing ATPase activity at concentrations ranging from 0.1 mM to 5 mM. ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
peptide inhibitors derived from amino acid sequence of motif VI analyzed, binding of the inhibitory peptides does not interfere with the NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
wild-type and mutant, NTPase activity analyzed, functional binding of RNA analyzed
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the amino acids Arg185, Arg202 and Asn417 are critical for phosphohydrolysis
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
unwinding activity specific for single-strand paired RNA, does not unwind dsRNAs
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
unwinding of dsRNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Classical swine fever virus CSFV
Q9YS30
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Dengue virus PL046
-
-, NS3 C-terminal domain catalyzes ATP hydrolysis in the presence of MgCl2 or MnCl2. MgCl2 is more effective than MnCl2 at inducing ATPase activity at concentrations ranging from 0.1 mM to 5 mM. ATP hydrolysis is required for the unwinding activity of DENV NS3H, wild-type and mutant, NTPase activity analyzed, functional binding of RNA analyzed
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
West Nile virus WNV
-
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
Q08211
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
NTPase activity
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 85% of the activity with ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
P47047
ATP and dATP are the preferred nucleotide substrates. In the presence of ATP or dATP Mtr4p unwinds the duplex region of a partial duplex RNA substrate in the 3' to 5' direction. Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-, EF409381
either ATP or dATP is required for the unwinding activity
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
Q9M6R6, -
either ATP or dATP is required for the unwinding activity, VrRH1 catalyzes unwinding of a double-stranded RNA
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 10% of the activity with ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 25% of the activity with ATP
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 10% of the activity with ATP
-
-
?
dTTP + H2O
dTDP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 55% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Q08211
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
NTPase activity
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 55% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
49% of the phosphohydrolase activity with ATP
-
-
?
N1-methyl-ATP + H2O
N1-methyl-ADP + phosphate
show the reaction diagram
-
66% of the phosphohydrolase activity with ATP
-
-
?
N1-methyl-GTP + H2O
N1-methyl-GDP + phosphate
show the reaction diagram
-
49% of the phosphohydrolase activity with ATP
-
-
?
N6-methyl-ATP + H2O
N6-methyl-ADP + phosphate
show the reaction diagram
-
43% of the phosphohydrolase activity with ATP
-
-
?
O6-methyl-GTP + H2O
O6-methyl-GDP + phosphate
show the reaction diagram
-
17% of the phosphohydrolase activity with ATP
-
-
?
ribavirin triphosphate + H2O
ribavirin diphosphate + phosphate
show the reaction diagram
-
36% of the phosphohydrolase activity with ATP
-
-
?
RNA + H2O
?
show the reaction diagram
-
-
-
-
?
RNA + H2O
?
show the reaction diagram
-
helicase/unwinding activity
-
-
?
RNA + H2O
?
show the reaction diagram
-, EF409381
helicase/unwinding activity, either ATP or dATP is required for the unwinding activity
-
-
?
RNA + H2O
?
show the reaction diagram
-
RNA unwinding activity, the enzyme contains two RecA-like domains, opening and closing of the interdomain cleft during RNA unwinding
-
-
?
RNA + H2O
?
show the reaction diagram
-
helicase/unwinding activity, ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
RNA + H2O
?
show the reaction diagram
-, Q9YS30
NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview
-
-
?
RNA + H2O
?
show the reaction diagram
-
RNA helicase actiivty
-
-
?
RNA + H2O
?
show the reaction diagram
-
RNA unwinding activity, substrate is a 154mer of 23S rRNA generated by T7 polymerase from in vitro transcription
-
-
?
RNA + H2O
?
show the reaction diagram
Q9WPH5
unwinding helicase activity, NS3 is ahighly basic protein with multiple RNA binding sites
-
-
?
RNA + H2O
?
show the reaction diagram
Classical swine fever virus CSFV
Q9YS30
NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview
-
-
?
RNA + H2O
?
show the reaction diagram
Dengue virus PL046
-
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
Q08211
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
NTPase activity
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-, Q9YS30
helicase activity is about 55% of the activity with ATP
-
-
?
XTP + H2O
XDP + phosphate
show the reaction diagram
-
40% of the phosphohydrolase activity with ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
49% of the phosphohydrolase activity with ATP
-
-
?
additional information
?
-
-
BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview
-
-
-
additional information
?
-
-
nonstructural proteins NS3 and NS5 form complexes in infected mammalian cells
-
-
-
additional information
?
-
-
the enzyme is involved in viral replication
-
-
-
additional information
?
-
-
the enzyme plays an important role in viral replication, multifunctional enzyme showing protease, helicase, and NTPase activities
-
-
-
additional information
?
-
-
multifunctional enzyme showing protease, helicase, and NTPase activities, the enzyme has a function in RNA replication complex assembly besides its function in RNA synthesis/capping, the enzyme activity is located in the C-terminal nucleoside triphosphatase/helicase domain of the BMV 1a protein RNA replication factor
-
-
-
additional information
?
-
-
substrate specificity, bifunctional enzyme, NS3 is an RNA-stimulated nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase, overview, the full-length NS3 with or without NS2B cofactor domain exhibits a catalytically more efficient RNA helicase activity than the N-terminally-truncated NS3 helicase domain, suggesting that the protease domain enhances RNA helicase activity
-
-
-
additional information
?
-
-
the multifunctional enzyme shows RNA-dependent NTPase and helicase activities, no activity with ADP and AMP
-
-
-
additional information
?
-
-, Q9YS30
nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus
-
-
-
additional information
?
-
P03314
NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping
-
-
-
additional information
?
-
-
the enzyme is unable to unwind duplex DNA
-
-
-
additional information
?
-
-
the mature NS3 protein comprises 5 domains: the N-terminal 2 domains form the serine protease along with the NS4A cofactor, and the C-terminal 3 domains form the helicase. The helicase portion of NS3 can be separated form the protease portion by cleaving a linker. Since the protease portion is more hydrophobic, removing it allows the NS3 helicase fragment to be expressed as a more soluble protein at higher levels in Escherichia coli. The fragment of NS3 possessing helicase activity is referred to as HCV helicase
-
-
-
additional information
?
-
-, EF409381
DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
-
-
-
additional information
?
-
-
helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities
-
-
-
additional information
?
-
-
NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
-
-
-
additional information
?
-
-, Q9YS30
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
-
-
-
additional information
?
-
Q9WPH5
the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
-
-
-
additional information
?
-
-
the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
-
-
-
additional information
?
-
-
The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins
-
-
-
additional information
?
-
-
conformational changes during ATP hydrolysis and RNA unwinding: on ssRNA binding, the NS3 enzyme switches to a catalytic competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis. Determination of enzyme structure-function relationship of enzyme bound to single-stranded RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent, reaction mechanism and RNA recognition, overview. RNA-unwinding mechanism, overview
-
-
-
additional information
?
-
-
NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain
-
-
-
additional information
?
-
-
open helicase conformation in the absence of nucleotides, or in the presence of ATP, or ADP, or RNA. In the presence of ADP and RNA, the open conformation is retained. By contrast, cooperative binding of ATP and RNA leads to a compact helicase structure, direct transitions between open and closed conformations, overview
-
-
-
additional information
?
-
-
RhlB is the only Escherichia coli DEAD box protein that requires a protein partner to stimulate its ATPase activity
-
-
-
additional information
?
-
-
the C-terminal region of NS3 forms the RNA helicase domain, an ATP-driven molecular motor
-
-
-
additional information
?
-
-
the helicase domain of Dengue virus NS3 protein, i.e. DENV NS3H, contains RNA-stimulated nucleoside triphosphatase, NTPase, ATPase/helicase, and RNA 5'-triphosphatase, RTPase, activities that are essential for viral RNA replication and capping. A 5'-tailed RNA is a better RTPase substrate than an RNA containing no 5'-dangling nucleotide
-
-
-
additional information
?
-
P17844
DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
-
-
-
additional information
?
-
-
human telomerase RNA interacts with the N-terminal domain of RHAU
-
-
-
additional information
?
-
-
p68 interacts with an intronic splicing activator, RNA binding motif protein 4 (RBM4), thereby stimulating tau exon 10 inclusion
-
-
-
additional information
?
-
-
recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs
-
-
-
additional information
?
-
-
RNA helicase A interacts with La ribonucleoprotein domain family member 6 (LARP6) which recruits RHA to the 5' UTR of collagen mRNAs
-
-
-
additional information
?
-
-
using yeast two-hybrid and pull-down assays it is shown that RH22 interacts with the 50S ribosomal protein RPL24
-
-
-
additional information
?
-
Classical swine fever virus CSFV
Q9YS30
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
-
-
-
additional information
?
-
Dengue virus PL046
-
the helicase domain of Dengue virus NS3 protein, i.e. DENV NS3H, contains RNA-stimulated nucleoside triphosphatase, NTPase, ATPase/helicase, and RNA 5'-triphosphatase, RTPase, activities that are essential for viral RNA replication and capping. A 5'-tailed RNA is a better RTPase substrate than an RNA containing no 5'-dangling nucleotide
-
-
-
additional information
?
-
Rice hoja blanca virus RHBV
-
the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
-
-
-
additional information
?
-
West Nile virus WNV
-
NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication, NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O60231
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27395
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-, EF409381
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes. GRTH has a negative role on its mRNA stability
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P47047
Mtr4p can unwind duplex RNA in the presence of ATP and a single-stranded RNA tail in the 3' to 5' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
phosphohydrolase and helicase activities of NPH-II are essential for virus replication
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RHA is a coactivator in STAT6-mediated transcription, and this function is dependent on its helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O15523, Q9NQI0, Q9UHL0
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q501J6, Q61656, Q9QY15
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9QY16
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q501J6, Q61656, Q9QY15
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O15523, Q9NQI0, Q9UHL0
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P06634
the DEAD-box protein DED1 has the ability to balance RNA unwinding with a profound strand annealing activity in a highly dynamic fashion
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
RNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
NTPase activity analyzed, ambiguous helicase activity, enzyme capable for unwinding RNA and DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9WPH5
RNA-stimulated ATPase activities determined, interaction between the replicative component nonstructural protein 3 (NS3) with the nonstructural protein 4A (NS4A)
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27958
the Arg-rich amino acid motif HCV1487-1500, a fragment of domain 2 NS3 of Hepatitis C virus, as well as the complete domain 2, and domain 2 lacking the flexible loop localized between Val1458 and Thr1476, mediate competitive inhibition of diverse protein kinase C functions, inhibition of rat brain PKC, overview
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Dengue virus PL046
-
-
-
-
?
RNA + H2O
?
show the reaction diagram
-
-
-
-
?
RNA + H2O
?
show the reaction diagram
-
helicase/unwinding activity
-
-
?
RNA + H2O
?
show the reaction diagram
-, EF409381
helicase/unwinding activity, either ATP or dATP is required for the unwinding activity
-
-
?
RNA + H2O
?
show the reaction diagram
-
RNA unwinding activity, the enzyme contains two RecA-like domains, opening and closing of the interdomain cleft during RNA unwinding
-
-
?
RNA + H2O
?
show the reaction diagram
Dengue virus PL046
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
West Nile virus WNV
-
-
-
-
?
additional information
?
-
-
BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview
-
-
-
additional information
?
-
-
nonstructural proteins NS3 and NS5 form complexes in infected mammalian cells
-
-
-
additional information
?
-
-
the enzyme is involved in viral replication
-
-
-
additional information
?
-
-
the enzyme plays an important role in viral replication
-
-
-
additional information
?
-
-, EF409381
DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
-
-
-
additional information
?
-
-
helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities
-
-
-
additional information
?
-
-
NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
-
-
-
additional information
?
-
-, Q9YS30
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
-
-
-
additional information
?
-
Q9WPH5
the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
-
-
-
additional information
?
-
-
the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
-
-
-
additional information
?
-
-
The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins
-
-
-
additional information
?
-
P17844
DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
-
-
-
additional information
?
-
-
human telomerase RNA interacts with the N-terminal domain of RHAU
-
-
-
additional information
?
-
-
p68 interacts with an intronic splicing activator, RNA binding motif protein 4 (RBM4), thereby stimulating tau exon 10 inclusion
-
-
-
additional information
?
-
-
recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs
-
-
-
additional information
?
-
-
RNA helicase A interacts with La ribonucleoprotein domain family member 6 (LARP6) which recruits RHA to the 5' UTR of collagen mRNAs
-
-
-
additional information
?
-
-
using yeast two-hybrid and pull-down assays it is shown that RH22 interacts with the 50S ribosomal protein RPL24
-
-
-
additional information
?
-
Classical swine fever virus CSFV
Q9YS30
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
-
-
-
additional information
?
-
Rice hoja blanca virus RHBV
-
the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
-
-
-
additional information
?
-
West Nile virus WNV
-
NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activity 3-5-fold lower when magnesium ions are replaced by
KCl
-
slight stimulation at 0.05-0.1 M, inhibition at 0.2 M
Mg2+
-
preferred metal ion, ATPase activity
Mg2+
-
metal-dependent NTPase activity, mechanism involves a bound sulfate ion
Mg2+
-
required for ATPase activity
Mg2+
P27395
no ATPase activity of the wild-type in the absence of
Mg2+
-
activates, binding complexes, overview
Mg2+
-
divalent cation required, Ca2+ or Mn2+ do not substitute for Mg2+
Mg2+
-
requirement for divalent ions for ATP hydrolysis is specific for Mg2+ and is not supported by Mn2+ and Ca2+. Half-maximum activity is achieved with concentrations of Mg2+ of 0.120 mM
Mg2+
-, EF409381
activates
Mg2+
-, Q9YS30
activates; the helicase activity requires divalent ions. Mn2+ is preferred over Mg2+
Mg2+
-
can be substituted by a Mn2+ ion for the enzymatic reaction
Mg2+
-
maximal NTPase activity achieved in the presence of 1.5-2 mM MgCl2
Mg2+
-
activates, preferred metal ion; activity depends on divalent cations, assay concentration 1.5 mM, rate of ATP hydrolysis 10 times enhanced with Mg2+ as divalent cation cofactor, rate of ATP hydrolysis increases slightly when the NaCl concentration is elevated in the range of 10 mM and 200 mM
Mg2+
-
activates
Mg2+
-
activates
Mg2+
-
activates
Mn2+
-
can substitute partially for Mg2+, ATPase activity
Mn2+
-, Q9YS30
the helicase activity requires divalent ions. Mn2+ is preferred over Mg2+
Mn2+
-
can substitute for a Mg2+ ion in the enzymatic reaction
Mn2+
-
activity 3-5-fold lower when magnesium ions are replaced by
NaCl
-
stimulates at 300-500 mM
NaCl
-
slightly activating ATPase activity at 10-200 mM, and RTPase at 15-50 mM
Ni2+
-
activity 3-5-fold lower when magnesium ions are replaced by
sulfate
-
bound, required for the metal-dependent NTPase reaction mechanism
Zn2+
-
activity 3-5-fold lower when magnesium ions are replaced by
Mn2+
-
activates; activity depends on divalent cations, assay concentration 1.5 mM, rate of ATP hydrolysis more than 100 times over basal levels with Mn2+ as divalent cation cofactor
additional information
-
no or poor effect by Mn2+, Zn2+, Co2+, Ca2+, and Ni2+
additional information
-
the ATPase activity requires a divalent cation cofactor to function but is not sensitive to high ionic strength
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2',3'-ddATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2',3'-ddGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2',3'-ddTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2',3'-dideoxy-ATP
-
-
2',3'-dideoxy-GTP
-
-
2'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2'-Deoxy-ATP
-
-
2'-deoxy-GTP
-
-
2'-deoxy-L-GTP
-
-
-
2'-deoxythymidine 5'-phosphoryl-beta,gamma-hypophosphate
-
i.e. ppopT, dTTP analogue, most efficient inhibitor of NTPase activity among nucleotide derivaties, inhibits the ATP-dependent helicase reaction and also the ATP-independent duplex unwinding, structure of nucleic base and ribose fragment of NTP molecule have a slight effects on inhibitory properties
2'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2'-dTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2'-fluoro-2'-deoxy-ATP
-
-
-
2-amino-ATP
-
-
2-hydroxy-ATP
-
-
-
3'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
3'-deoxy-ATP
-
-
3'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
3'-dUTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
6-methyl-thio-ITP
-
-
-
7-methyl-GTP
-
-
8-bromo-ATP
-
-
ADP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
AMP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
ATP-gamma-S
-
5.4 mM, about 50% of the original helicase activity is inhibited, competitive inhibitor
benzoyl-Nle-Lys-Arg-Arg
-
competitive inhibition, structure-activity relationship
beta,gamma-methylene-ATP
-
efficient inhibitor, like the N1-oxides N1-O-ATP and N1-OH-ITP
Cu2+
-
inhibits ATPase activity, IC50: 0.13 mM
dATP
-
inhibits unwinding
Fe2+
-
inhibits ATPase activity, IC50: 0.75 mM
-
GTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
Hg2+
-
inhibits ATPase activity, IC50: 49 nM, targets the cysteine residue in the DECH box, competitive, cysteine or DTT protect at large concentrations
Imidodiphosphate
-
maximal inhibitory activity among diphosphate analogues, non-catalytic and catalytic conditions, inhibits the ATP-dependent helicase reaction but no effect on the ATP-independent duplex unwinding, structure of nucleic base and ribose fragment of NTP molecule have a slight effects on inhibitory properties
KCl
-
slight stimulation at 0.05-0.1 M, inhibition at 0.2 M
KCl
-
RNA-dependent ATPase activity is sensitive to high salt concentrations. Maximal activity is obtained in the absence of KCl, and it is inhibited 50% at 0.1 M KC1, completely inhibited at 0.3 M KCl
KCl
-
slight decrease of activity in presence of
N1-methyl-ATP
-
-
N1-methyl-GTP
-
-
-
N1-O-ATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
N1-OH-ITP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
N6-methyl-ATP
-
-
NEM
-
5 mM, ATPase activity is blocked
PCMB
-
inhibits ATPase activity, IC50: 88 nM
ribavirin triphosphate
-
-
tetrabromobenzotriazole
-
inhibits unwinding, no inhibition of ATP hydrolysis
UTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
additional information
-
no or poor inhibition by Mn2+, Zn2+, Co2+, Ca2+, and Ni2+
-
additional information
-
inhibitory potential of sequences of NTPase/helicase motifs VI derived peptides and their deleted derivatives analyzed, NTP-binding and hydrolyzing site not involved
-
additional information
P27958
domain 2 of wild-type NS3 protein and domain 2 devoid of the loop structure used for inhibition studies on functions of protein kinase C (PKC), inhibitory potential towards the majority of protein kinase C isoforms shown
-
additional information
-
several extracts of marine organisms exhibit different inhibitory effects on the RNA and DNA helicase activities of HCV NS3
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Deoxyribonucleotides
-, EF409381
ATPase activity of the bacterially expressed BmL3-helicase is triggered by both the ssRNA and the dsRNA and, to a much lesser extent, by the ssDNA and dsDNA
-
Double-stranded DNA
-, EF409381
weak stimulation
Double-stranded RNA
-, EF409381
ATPase activity of the recombinant BmL3-helicase is strongly stimulated by dsRNA
-
nonstructural protein 4A
-
i.e. NS4A, stimulates serine protease activity of NS3 protein, helicase domain enhances serine protease activity and vice versa
-
nonstructural protein 4A
Q9WPH5
i.e. NS4A, enhances the coupling between RNA binding and ATPase activity of nonstructural protein 3 (NS3), does not influence the kinetic parameters for RNA unwinding by NS3; NS4A binds to the NS3 protease domain and serves as an obligate cofactor for NS3 serine protease activity, thus NS4A enhances the ability of the C-terminal helicase to bind RNA in presence of ATP acting as a cofactor for helicase activity, 100fold lower Km of NS3 with RNA in presence of NS4A. NS4A mutants that are defective in ATP-coupled RNA binding sre lethal in vivo
-
nonstructural protein 5
-
interaction with NS5, the viral RNA-dependent RNA polymerase, stimulates NS3 NTPAse and RTPase activities as well as thr RNA helicase activity
-
poly(C)
P0C6X1
strong stimulation of ATPase activity
poly(C)
-
stimulates ATPase and dATPase activity
Poly(dA)
P0C6X1
strong stimulation of ATPase activity
Poly(dT)
P0C6X1
strong stimulation of ATPase activity
Poly(rU)
-
stimulates the ATPase activity of NS3
Poly(U)
P0C6X1
strong stimulation of ATPase activity
polyU
-
stimulatory effect of polyU on ATP hydrolysis is significantly attenuated when NaCl concentration is 50 mM or higher, functional binding of polyU mainly through electrostatic interaction, binding triggers a conformational rearrangement that activates the catalytic core of the enzyme for ATP hydrolysis
ribonucleotides
-, EF409381
ATPase activity of the bacterially expressed BmL3-helicase is triggered by both the ssRNA and the dsRNA and, to a much lesser extent, by the ssDNA and dsDNA, recombinant BmL3-helicase is strongly stimulated by dsRNA
-
RNA
-
RNA-stimulated enzyme
RNA
-
the ATPase activity is stimulated by the presence of RNA and single-stranded DNA molecules
RNase E
-
is required for ATPase and RNA unwinding activities of the enzyme, forms a complex with the enzyme, interaction analysis, overview. Avid, enthalpy-favored interaction between the helicase and RNase E 696-762 with an equilibrium binding constant Kaof at least 1 x 108 M-1 determined by isothermal titration calorimetry. Protein-protein and RNA-binding surfaces both communicate allosterically with the ATPase catalytic center
-
rRNA
-
activates the ATPase activity of DbpA by promoting a conformational change after ATP binding that is associated with hydrolysis
Single-stranded DNA
-
on single-stranded RNA binding, the NS3 enzyme switches to a catalytic competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis
Single-stranded DNA
-, EF409381
weak stimulation
Single-stranded DNA
-
the ATPase activity is stimulated by the presence of RNA and single-stranded DNA molecules
Single-stranded RNA
-
RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
Single-stranded RNA
P47047
stimulates
Single-stranded RNA
-, EF409381
stimulates
single-strandede DNA
-
stimulates
-
tRNA
P47047
stimulates
MLN51
P38919
stimulates the RNA-helicase activity of eIF4AIII
-
additional information
-
NS3 requires the hydrophilic domain of NS2B for activation
-
additional information
P0C6X1
no stimulation by poly(G) of ATPase activity
-
additional information
P47047
a 20-bp duplex RNA is ineffective in stimulating the (d)ATPase activity of Mtr4p
-
additional information
P26663
low salt conditions enhance unwinding by monomeric NS3
-
additional information
-, Q9YS30
the NS3 protease domain enhances the helicase activity of NS3 but has no effect on its NTPase activity. For the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000001
-
ATP
Q9WPH5
pH 6.5, 37C, RNA-stimulated ATPase activity of mutant NS3-4A
0.000002
-
ATP
Q9WPH5
pH 6.5, 37C, RNA-stimulated ATPase activity of mutant S1369R/M1708A
0.0001
-
ATP
Q9WPH5
pH 6.5, 37C, RNA-stimulated ATPase activity of wild-type NS3
0.0005
-
ATP
Q9WPH5
pH 6.5, 37C, RNA-stimulated ATPase activity of mutant M1708A; pH 6.5, 37C, RNA-stimulated ATPase activity of mutant Y1702A
0.001
-
ATP
Q9WPH5
RNA-stimulated ATPase activity, recombinant protein, NS3-4A construct; RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R mutant
0.002
-
ATP
Q9WPH5
RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R/M1708A mutant
0.0095
-
ATP
-
pH 7.5, 37C, native WNV NS3 protein purified from infected cells
0.013
-
ATP
-
recombinant protein including C-terminal portion the ATPase/helicase domain encompassing residues 181-619, ATP concentration 1mM ATP, ATPase but not RNA helicase activity
0.0157
-
ATP
-
pH 7.6, 37C
0.03
-
ATP
Q9WPH5
RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R/Y1702A mutant
0.05
-
ATP
Q9WPH5
RNA-stimulated ATPase activity, recombinant protein, NS3-4A M1708A mutant; RNA-stimulated ATPase activity, recombinant protein, NS3-4A Y1702A mutant
0.1
-
ATP
Q9WPH5
RNA-stimulated ATPase activity, NS3, recombinant protein
0.13
-
ATP
-
pH 7.5, 37C, recombinant C-terminal portion of the NS3
0.14
-
ATP
-
pH 7.5, 37C, wild-type enzyme
0.163
-
ATP
-
addition of polyuridylate lowers Km for the ATP substrate
0.18
-
ATP
-
pH 7.5, 37C, mutant enzyme D172A; pH 7.5, 37C, mutant enzyme F179A
0.2
-
ATP
-
pH 7.5, 37C, mutant enzyme E173A; pH 7.5, 37C, mutant enzyme R170A
0.22
-
ATP
-
pH 7.5, 37C, mutant enzyme E169A
0.24
-
ATP
P38919
pH 7.5, 25C, in absence of MLN51
0.24
-
ATP
-
pH 7.5, 37C, mutant enzyme E180A
0.256
-
ATP
-
wild-type
0.27
-
ATP
-
pH 7.5, 37C, mutant enzyme E182A
0.34
-
ATP
-
pH 7.5, 30C, wild-type enzyme
0.39
-
ATP
P47047
pH 7.5, 37C
0.39
-
ATP
-
pH 7.5, 37C, mutant enzyme K186A
0.51
-
ATP
-
pH 7.5, 30C, mutant enzyme T166A
0.64
-
ATP
-
pH 7.5, 37C, mutant enzyme Q188A
0.66
-
ATP
-
pH 7.5, 30C, mutant enzyme T166S
0.78
-
ATP
-
pH 7.5, 30C, mutant enzyme F162L
0.94
-
ATP
-
pH 7.5, 37C, mutant enzyme K187A
1.1
-
ATP
-
pH 7.5, 30C, mutant enzyme Q169E
3.5
-
ATP
-
pH 7.5, 30C, mutant enzyme F162A
33
-
ATP
-
pH 7.5, 30C, mutant enzyme Q169A
0.09
-
GTP
-
pH 7.5, 37C, mutant enzyme F179A; pH 7.5, 37C, mutant enzyme K187A
0.1
-
GTP
-
pH 7.5, 37C, mutant enzyme K186A
0.11
-
GTP
-
pH 7.5, 37C, mutant enzyme E173A
0.23
-
GTP
-
pH 7.5, 37C, mutant enzyme E182A
0.27
-
GTP
-
pH 7.5, 37C, mutant enzyme E180A; pH 7.5, 37C, mutant enzyme R170A
0.29
-
GTP
-
pH 7.5, 37C, mutant enzyme Q188A
0.33
-
GTP
-
pH 7.5, 37C, mutant enzyme D172A
0.34
-
GTP
-
pH 7.5, 37C, mutant enzyme E169A
0.000114
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutant S108C/S229C
0.000156
-
RNA
-
pH 7.5, 37C, native wild-type enzyme
0.00017
-
RNA
-
pH 7.5, 37C, recombinant wild-type YxiN
0.000324
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutantA115C/S229C
0.000422
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutantA115C/D262C
0.000458
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutant S108C/E224C
0.000496
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutantA115C/E224C
0.35
-
GTP
-
pH 7.5, 37C, wild-type enzyme
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
protease activities of NS3-4A variants analyzed, uncleaved NS3/4A polyprotein lacks protease and helicase activities
-
additional information
-
additional information
Q9WPH5
kinetics of wild-type and mutant enzymes, overview; RNA-stimulated ATPase activities of NS3-4A variants analyzed, functionally important ATP-bound state of NS3 binds RNA much more tightly in the presence of NS4A, effectively coupling RNA binding to ATPase activity
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.043
-
ATP
-
pH 7.5, 30C, mutant enzyme Q169E
0.3
-
ATP
-
pH 7.5, 30C, mutant enzyme F162A
0.58
-
ATP
-
pH 7.5, 37C, mutant enzyme D172A
0.92
-
ATP
-
pH 7.5, 37C, mutant enzyme E173A
1
-
ATP
-
pH 7.5, 30C, mutant enzyme Q169A
1
-
ATP
-
pH 7.5, 37C, mutant enzyme R170A
1.1
-
ATP
-
pH 7.5, 37C, mutant enzyme E180A
1.2
-
ATP
-
pH 7.5, 37C, mutant enzyme F179A
1.25
-
ATP
-
pH 7.5, 37C, mutant enzyme E169A
1.8
-
ATP
-
pH 7.5, 30C, mutant enzyme T166S
2
-
ATP
-
pH 7.5, 30C, mutant enzyme F162L; pH 7.5, 30C, mutant enzyme T166A
2.2
-
ATP
-
pH 7.5, 37C, mutant enzyme K187A
2.7
-
ATP
-
pH 7.5, 37C, mutant enzyme K186A
3
-
ATP
-
pH 7.5, 37C, wild-type enzyme
3.3
-
ATP
-
pH 7.5, 37C, mutant enzyme E182A; pH 7.5, 37C, mutant enzyme Q188A
3.5
-
ATP
-
pH 7.5, 30C, wild-type enzyme
22.2
-
ATP
P47047
pH 7.5, 37C
0.92
-
GTP
-
pH 7.5, 37C, mutant enzyme D172A
1
-
GTP
-
pH 7.5, 37C, mutant enzyme K187A
1.1
-
GTP
-
pH 7.5, 37C, mutant enzyme E173A; pH 7.5, 37C, mutant enzyme F179A
1.3
-
GTP
-
pH 7.5, 37C, mutant enzyme E180A
1.7
-
GTP
-
pH 7.5, 37C, mutant enzyme K186A; pH 7.5, 37C, mutant enzyme Q188A; pH 7.5, 37C, mutant enzyme R170A
1.83
-
GTP
-
pH 7.5, 37C, mutant enzyme E169A
2.75
-
GTP
-
pH 7.5, 37C, wild-type enzyme
3.6
-
GTP
-
pH 7.5, 37C, mutant enzyme E182A
0.64
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutant S108C/S229C
0.85
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutant S108C/E224C
0.98
-
RNA
-
pH 7.5, 37C, recombinant wild-type YxiN
1.3
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutantA115C/S229C
1.4
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutantA115C/E224C
1.41
-
RNA
-
pH 7.5, 37C, recombinant YxiN mutantA115C/D262C
1.48
-
RNA
-
pH 7.5, 37C, native wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7
-
ATP
-
pH 7.5, 37C, mutant enzyme E180A
22040
2.3
-
ATP
-
pH 7.5, 37C, mutant enzyme K187A
22040
3.22
-
ATP
-
pH 7.5, 37C, mutant enzyme D172A
22040
4.6
-
ATP
-
pH 7.5, 37C, mutant enzyme E173A
22040
5
-
ATP
-
pH 7.5, 37C, mutant enzyme R170A
22040
5.2
-
ATP
-
pH 7.5, 37C, mutant enzyme Q188A
22040
5.68
-
ATP
-
pH 7.5, 37C, mutant enzyme E169A
22040
6.7
-
ATP
-
pH 7.5, 37C, mutant enzyme F179A
22040
6.9
-
ATP
-
pH 7.5, 37C, mutant enzyme K186A
22040
12.2
-
ATP
-
pH 7.5, 37C, mutant enzyme E182A
22040
21.43
-
ATP
-
pH 7.5, 37C, wild-type enzyme
22040
2.79
-
GTP
-
pH 7.5, 37C, mutant enzyme D172A
11186
4.8
-
GTP
-
pH 7.5, 37C, mutant enzyme E180A
11186
5.38
-
GTP
-
pH 7.5, 37C, mutant enzyme E169A
11186
5.9
-
GTP
-
pH 7.5, 37C, mutant enzyme Q188A
11186
6.3
-
GTP
-
pH 7.5, 37C, mutant enzyme R170A
11186
10
-
GTP
-
pH 7.5, 37C, mutant enzyme E173A
11186
11
-
GTP
-
pH 7.5, 37C, mutant enzyme K187A
11186
12
-
GTP
-
pH 7.5, 37C, mutant enzyme F179A
11186
15.7
-
GTP
-
pH 7.5, 37C, mutant enzyme E182A
11186
17
-
GTP
-
pH 7.5, 37C, mutant enzyme K186A
11186
22.26
-
GTP
-
pH 7.5, 37C, wild-type enzyme
11186
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.116
-
2',3'-ddATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.721
-
2',3'-ddGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.298
-
2',3'-ddTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.6
-
2',3'-dideoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.3
-
2',3'-dideoxy-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.291
-
2'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.6
-
2'-Deoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
3.4
-
2'-deoxy-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
1.3
-
2'-deoxy-L-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.097
-
2'-deoxythymidine 5'-phosphoryl-beta,gamma-hypophosphate
-
i.e. ppopT, dTTP analogue, inhibition of NTPase activity of NS3 protein by NTP derivatives
0.277
-
2'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.116
-
2'-dTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.4
-
2'-fluoro-2'-deoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.2
-
2-amino-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
2.4
-
2-hydroxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.141
-
3'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.5
-
3'-deoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.443
-
3'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.26
-
3'-dUTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.6
-
6-methyl-thio-ITP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
1
-
7-methyl-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.7
-
8-bromo-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.34
-
ADP
-
pH 7.5, 30C, mutant enzyme T166S
0.36
-
ADP
-
pH 7.5, 30C, mutant enzyme T166A; pH 7.5, 30C, wild-type enzyme
1.3
-
ADP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
3
-
ADP
-
pH 7.5, 30C, mutant enzyme F162L
5
-
AMP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.5
-
Ara-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.3
-
ATP
-
pH 7.5, 37C, wild-type enzyme
0.007
-
benzoyl-Nle-Lys-Arg-Arg
-
full-length enzyme in presence of cofactor CF40-Gly4-Ser-Gly4-NS3FL
0.145
-
beta,gamma-methylene-ATP
-
efficient inhibitor, like the N1-oxides N1-O-ATP and N1-OH-ITP
0.576
-
GTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
8.1
-
GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.9
-
ITP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
1.5
-
N1-methyl-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
2.6
-
N1-methyl-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.205
-
N1-O-ATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.109
-
N1-OH-ITP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.5
-
N6-methyl-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
2.3
-
ribavirin triphosphate
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
1.46
-
UTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.8
-
2',3'-dideoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.5
-
2',3'-dideoxy-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.9
-
2'-Deoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
1.8
-
2'-deoxy-L-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.5
-
2'-fluoro-2'-deoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.3
-
2-amino-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
3.3
-
2-hydroxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.7
-
3'-deoxy-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.8
-
6-methyl-thio-ITP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
2.7
-
6-thio-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
1.4
-
7-methyl-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.9
-
8-bromo-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.7
-
Ara-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.4
-
ATP
-
pH 7.5, 37C, wild-type enzyme
0.13
-
Cu2+
-
inhibits ATPase activity, IC50: 0.13 mM
0.75
-
Fe2+
-
inhibits ATPase activity, IC50: 0.75 mM
-
11
-
GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.000049
-
Hg2+
-
inhibits ATPase activity, IC50: 49 nM, targets the cysteine residue in the DECH box, competitive, cysteine or DTT protect at large concentrations
2
-
N1-methyl-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
3.5
-
N1-methyl-GTP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
-
0.7
-
N6-methyl-ATP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.000088
-
PCMB
-
inhibits ATPase activity, IC50: 88 nM
3.1
-
ribavirin triphosphate
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
0.06
-
tetrabromobenzotriazole
-
-
1.2
-
ITP
-
pH 7.5, 37C, wild-type enzyme, inhibition of the ATPase reaction
additional information
-
additional information
-
sequences of NTPase/helicase motifs VI derived peptides and their deleted derivatives analyzed, NTPase activity not affected
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00000001
-
-
about, wild-type enzyme, RNA helicase activity
additional information
-
-
specificities and activities of wild-type and mutant enzymes
additional information
-
-
RNA replication, RNA protection, spherule formation size, relative ATPase activity, RNA accumulation and stabilization, of wild-type and mutant enzymes, overview
additional information
-
P27395
structural characterization of catalytic domain, mutation analysis of residue substitution in the Walker A motif (Gly199, Lys200 and Thr201), within the NTP-binding pocket (Gln457, Arg461 and Arg464) and of Arg458 in the outside of the pocket in the motif IV, residues crucial for ATPase and RNA helicase activities and virus replication, Lys200 cannot be substituted by other residues to establish sufficient activities, structure of the NTP-binding pocket well conserved among the viruses of the Flaviviridae
additional information
-
-
helicase capable of unwinding duplex RNA or DNA, ambiguous
additional information
-
-
overview of sequences of NTPase/helicase motifs VI derived peptides and their deleted derivatives, kinetic analyses reveals that binding of the peptides do not interfere with the NTPase activity, peptides do not interact with the ATP binding site
additional information
-
-
structure of nucleic base and ribose fragment of NTP molecule has a slight effect on inhibitory properties
additional information
-
P27958
surface of domain 2 of the NS3 NTPase/helicase in direct vicinity to a flexible loop that is localized between Val1458 and Thr1476, accessibility of the Arg-rich amino acid motif by this loop for protein kinase C inhibition analyzed, two variants of domain 2 generated, in vitro protein kinase C (PKC) phosphorylation studies, binding and competition assays, modelling of ribbon diagrams, presence of the intact loop abolishes the binding of domain 2 to a tailed duplex RNA, binding of dsDNA not affected, loop structure reduces the extent of inhibition of protein kinase C (PKC) by domain 2 and regulates the binding of dsRNA, various mechanisms by which the NS3 protein perturb signal transduction in infected cells
additional information
-
-
biochemical properties and enzymatic activity of the RNA-helicase domain, functional characterization to get information about the flavivirus replication mechanism, NTPase-deficient mutant generated, RNA binding features, electrostatic interaction with RNA, basal ATPase activity insensitive to high ionic strength
additional information
-
-
the nonstructural protein 4A (NS4A) stimulates NS3 serine protease activity, truncated and full-length complexes between nonstructural protein 3 (NS3) and nonstructural protein 4A (NS4) purified, serine protease activities analyzed, NS3 protease domain enhances the RNA binding, ATPase, and RNA unwinding activities of the C-terminal NS3 helicase domain, isolated protease domain is much less reactive than full-length NS3, NS3 protease activity is enhanced by the presence of the NS3 helicase domain, indicating that the two domains have evolved to become completely interdependent
additional information
-
Q9WPH5
the nonstructural protein 4A (NS4A) enhances the ability of the N-terminal domain of NS3 protein to bind RNA in the presence of ATP, stimulates helicase activity, interaction between nonstructural protein 3 (NS3) and nonstructural protein 4A (NS4) mediated by amino acids of the C-terminus of NS4, mutation of the C-terminus of NS4 reduces ATP-coupled RNA binding, RNA binding studies, RNA-stimulated ATPase activity of N3-4a variants
additional information
-
-
structural characterization of the C-terminal portion containing the ATPase/helicase domain, encompasses residues 181-619, monomer structure determined by analytical centrifugation and gel filtration, SDS-PAGE and immunoblotting, structure determined by circular dichroism and fluorescence spectroscopy, ATPase activity stimulated by RNA and ssDNA, no RNA helicase activity at protein concentrations up to 500 nM, linker region between the protease and the helicase domains predicted as a prerequisite for protein-protein interactions leading to the formation of the active oligomer
additional information
-
-
development of continuous fluorescence assay based on fluorescence resonance energy transfer for the monitoring of RNA helicase activity in vitro. This assay will be useful for monitoring the detailed kinetics of RNA unwinding mechanisms and screening RNA helicase inhibitors at high throughput
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-, Q9YS30
ATPase assay at
6.5
-
Q9WPH5
ATPase and RNA binding assay at; helicase assay at
7
-
-
ATPase activity
7.2
-
P29562
assay at
7.4
-
-
ATPase assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
P47047
assay at
7.5
-
-, EF409381
assay at
7.5
-
Q9M6R6, -
assay at
7.5
-
P38919
assay at
7.5
-
-, Q9YS30
; RNA helicase assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
activity range, ATPase activity
6.5
-
-, Q9YS30
pH 6.5: about 50% of maximal activity, pH 8: about 80% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
P38919
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
ATPase assay at
37
-
P27395
assay at
37
-
P29562
assay at
37
-
P47047
assay at
37
-
-, EF409381
assay at
37
-
Q9M6R6, -
assay at
37
-
-, Q9YS30
assay at
37
-
-
assay at
37
-
Q9WPH5
ATPase and RNA binding assay at; helicase assay at
37
-
-
assay at
37
-
-
assay at
50
-
-
maximal ATPase activity and unwinding activity specific for single-strand paired RNA
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
50
-
40C: about 40% of maximal activity, 50C: optimum, 60C: less than 10% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
present in all blastomeres of the early embryo
Manually annotated by BRENDA team
Q501J6, Q61656, Q9QY15
DDX17 transcripts are abundant in rat brains in early embryonic stages and becomes downregulated in late post-natal and adults, suggesting involvement during neuronal differentiation during development of the central nervous system
Manually annotated by BRENDA team
B9VSG1, -
expressed in blastomeres and embryonic cells in planarian embryonic development
Manually annotated by BRENDA team
Q7ZX48
in the ciliary marginal zone adjacent to the neural retina and within the lens epithelium, present in the anterior eye during fibroblast growth factor 2 (FGF2)-mediated retinal regeneration. Ddx39 message is restricted to a subpopulation of proliferating cells in the developing and regenerating optic cup
Manually annotated by BRENDA team
Q501J6, Q61656, Q9QY15
high level of expression in male germ cells
Manually annotated by BRENDA team
-, EF409381
-
Manually annotated by BRENDA team
O15523, Q9NQI0
-
Manually annotated by BRENDA team
Q501J6, Q61656, Q9QY15
-
Manually annotated by BRENDA team
-
the 1 kb fragment (5' to the ATG codon) of GRTH gene contains sequences for androgen regulation of its expression in Leydig cells
Manually annotated by BRENDA team
Q7ZX48
developing limb buds at stages 4855
Manually annotated by BRENDA team
Q80YD1
low expression level
Manually annotated by BRENDA team
Q7ZX48
Ddx39 is present in the ventricular region of the developing neural tube up to and including stage 48
Manually annotated by BRENDA team
Q7ZX48
Ddx39 message is restricted to a subpopulation of proliferating cells in the developing and regenerating optic cup
Manually annotated by BRENDA team
Q9M6R6, -
VrRH1 may play a role in the viability of mung bean seeds
Manually annotated by BRENDA team
O15523, Q9NQI0
-
Manually annotated by BRENDA team
Q501J6, Q61656, Q9QY15
-
Manually annotated by BRENDA team
-
GRTH resides in the nucleus, cytoplasm and chromatoid body of round spermatids
Manually annotated by BRENDA team
O15523, Q9NQI0
-
Manually annotated by BRENDA team
Q501J6, Q61656, Q9QY15
-
Manually annotated by BRENDA team
O15523, Q9NQI0
expression is restricted to the male germ cell line; highly expressed in
Manually annotated by BRENDA team
Q501J6, Q61656, Q9QY15
highly expressed in
Manually annotated by BRENDA team
Q9QY16
highly expressed in
Manually annotated by BRENDA team
-
GRTH is a negative regulator of apoptosis in spermatocytes and promotes the progress of spermatogenesis
Manually annotated by BRENDA team
-
the expression of GRTH in testicular cells is differentially regulated by its 5' flanking sequence
Manually annotated by BRENDA team
Q80YD1
high expression level
Manually annotated by BRENDA team
Q7ZX48
facial mesenchyme
Manually annotated by BRENDA team
additional information
-
the virus is propagated in yeast cells
Manually annotated by BRENDA team
additional information
O15523, Q9NQI0
the protein is expressed in all tissues; vasa (DDX4) mRNA and protein are abundantly and specifically expressed in germ cells in both sexes throughout development
Manually annotated by BRENDA team
additional information
-, EF409381
presence of BmL3-helicase in various life stages of Brugia malayi
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
p68 shuttles between the nucleus and the cytoplasm. The nucleocytoplasmic shuttling of p68 is mediated by two nuclear localization signal and two nuclear exporting signal sequence elements. p68 shuttles via a classical RanGTPase dependent pathway
Manually annotated by BRENDA team
-
DDX3 and DDX5 both co-localize in the cytoplasm; DDX3 and DDX5 both co-localize in the cytoplasm
Manually annotated by BRENDA team
O60231
the GFP-DBP2 gene product, transiently expressed in HeLa cells, is localized in the nucleus
Manually annotated by BRENDA team
-
p68 predominately localizes in the cell nucleus
Manually annotated by BRENDA team
-
DDX5 is shutteld into the nucleus by DDX3
Manually annotated by BRENDA team
-
Vasa associates with the spindle and the separating sister chromatids at metaphase, and then disappears after telophase
Manually annotated by BRENDA team
additional information
-
BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Reovirus type 1 (strain Lang)
Reovirus type 3 (strain Dearing)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Vaccinia virus (strain Western Reserve)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
54000
-
P27395
molecular mass of the helicase/NTPase domain, SDS-PAGE
66000
-
-
recombinant protein of C-terminal portion the ATPase/helicase domain, residues 181-619, SDS-PAGE, gel filtration
130000
-
-
glycerol gradient centrifugation
140000
-
-
MALDI-TOF mass spectrometry
140000
-
-
MALDI-TOF
246000
-
-
calculated from sequence. Apart from an N-terminal domain of unknown function, Brr2p consists of two putative helicase domains, each connected at its C-terminus to a Sec63-like domain
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 49800, recombinant C-terminal helicase domain (amino-acid sequence corresponding to that between residues 189 and 620 of the predicted NS3 polypeptide), SDS-PAGE
?
-
x * 100000, gel filtration
?
-
x * 70000, His-tagged enzyme, SDS-PAGE
?
O60231
x * 119037, calculated from sequence
?
-
x * 66000, recombinant NS3, SDS-PAGE, x * 109000, recombinant MBP-fusion NS3 protein, SDS-PAGE
?
Rice hoja blanca virus RHBV
-
x * 66000, recombinant NS3, SDS-PAGE, x * 109000, recombinant MBP-fusion NS3 protein, SDS-PAGE
-
dimer
-
crystal structure, three-domain structure with asymmetric distribution of charges on the surface and a tunnel structure for RNA substrate access, overview
monomer
-
1 * 130000, SDS-PAGE
monomer
-
DbpA is monomeric in solution up to a concentration of 25 mM and over the temperature range of 4C to 22C
monomer
-
alphabeta, 29% alpha-helix, 15% beta-sheet, and 56% non-regular structures, globular monomer accounts for 90%, a small percentage (7%) of dimers or trimers, higher oligomers almost absent (3%), analytical centrifugation and gel filtration; in solution, x * 66000, about, recombinant soluble His6-tagged C-terminal portion of NS3, SDS-PAGE
monomer
West Nile virus WNV
-
alphabeta, 29% alpha-helix, 15% beta-sheet, and 56% non-regular structures, globular monomer accounts for 90%, a small percentage (7%) of dimers or trimers, higher oligomers almost absent (3%), analytical centrifugation and gel filtration; in solution, x * 66000, about, recombinant soluble His6-tagged C-terminal portion of NS3, SDS-PAGE
-
additional information
-
DEN2 nonstructural protein 3, NS3, has a serine protease domain and requires the hydrophilic domain of NS2B for activation
additional information
-
the enzyme activity is located in the C-terminal nucleoside triphosphatase/helicase domain of the BMV 1a protein RNA replication factor, BMV 1a protein contains an N-terminal capping domain with m7G-methyltransferase and m7GMP binding activities, and a C-terminal NTPase/helicase-like domain, comprising residues 562-961, containing 7 conserved helicase motifs, the two domains are separated by a proline-rich region, overview
additional information
-
the C-terminal region of NS3 forms the RNA helicase domain. The ATP binding site is housed between these two subdomains, structure modelling, overview
additional information
-
the C-terminal domain of the enzyme contains the Walker A and Walker B motifs, i.e. motif I, GK(S/T) and motif II, DExD/H
additional information
-
location of the nine conserved sequence motifs in the DEAD box helicase RhlB, structure modelling, overview
additional information
-
the linker region plays a critical role in determining the protein-protein interactions that leads to the formation of the active oligomer
additional information
Dengue virus PL046
-
the C-terminal domain of the enzyme contains the Walker A and Walker B motifs, i.e. motif I, GK(S/T) and motif II, DExD/H
-
additional information
West Nile virus WNV
-
the linker region plays a critical role in determining the protein-protein interactions that leads to the formation of the active oligomer
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
enzyme contains a 58-amino acid transit peptide that is predicted to be targeted to the chloroplast
phosphoprotein
O15523, Q9NQI0
helicase activity of DDX5 is regulated by phosphorylation and calmodulin binding
phosphoprotein
-
phosphorylation of p68 RNA helicase at Y593 upregulates transcription of the Snail1 gene
phosphoprotein
-
phosphorylation at serine/threonine residues of both DDX3 and DDX5 affect the protein-protein interaction. During the G2/M phase, phosphorylation of DDX3 is decreased, whereas, the phosphorylation of DDX5 is, compared with the G1/S phase; phosphorylation at serine/threonine residues of both DDX3 and DDX5 affect the protein-protein interaction. During the G2/M phase, phosphorylation of DDX3 is decreased, whereas, the phosphorylation of DDX5 is, compared with the G1/S phase
phosphoprotein
Q501J6, Q61656, Q9QY15
helicase activity of DDX5 is regulated by phosphorylation and calmodulin binding; helicase activity of DDX5 is regulated by phosphorylation and calmodulin binding; helicase activity of DDX5 is regulated by phosphorylation and calmodulin binding
phosphoprotein
Q9QY16
helicase activity of DDX5 is regulated by phosphorylation and calmodulin binding
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour diffusion method, crystallization of native enzyme, enzyme in complex with adenylyl imidodiphosphate, enzyme in complex with ADP, enzyme in complex with single-stranded RNA and enzyme in complex with single-stranded RNA and ADP; purified recombinant His-tagged catalytic domain of the NS3, hanging drop vapour diffusion method, at 13C over a well solution containing 0.1M MES, pH 6.5, and 20% PEG 3350, X-ray diffraction structure determination and analysis. Crystals for the AMPPNP complex are obtained by cocrystallization of NS3h at 5 mg/ml with 5 mM MnCl2 and 5 mM AMPPNP using a precipitating solution containing 0.1M MES, pH 6.5, and 10% PEG 3350, at 13C. Crystals with ADP are obtained by cocrystallization at a concentration of 2.5 mg/ml with 5 mM MnCl2 and 5 mM ADP in 0.1 M Tris-HCl, pH 7.0, and 7.5% PEG 3350 at 23C, further preparation of ternary complexes,overview
-
purified catalytic domain fragment, hanging drop vapour diffusion method, 0.002 ml of 10 mg/ml protein in 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 14% PEG 8000, mixed with an equal volume of precipitation solution, 18C, macroseeding, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
crystals of DDX1954-475 in complex with RNA and Mg/adenosine 5'-(beta,gamma-imido)triphosphate are obtained by vapor diffusion in sitting drops incubated at 4C by mixing 0.0001 ml of protein solution (20 mg/ml) including 10-molar excess of decauracil ssRNA, adenosine 5'-(beta,gamma-imido)triphosphate, and MgCl2 and 0.0002 ml of reservoir solution containing 14% polyethylene glycol monomethyl ether 2000, 0.25 M trimethylamine n-oxide, 0.1 M Tris, pH 8. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an alpha-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity
Q9UMR2
hanging-drop method, crystallization of recombinant DDX3 RNA helicase domain
-
sitting-drop vapor diffusion method at 4 C. Crystal structures of the conserved domain 1 of the DEIH-motif-containing helicase DHX9 and of the DEAD-box helicase DDX20. Both contain a RecA-like core, but DHX9 differs from DEAD-box proteins in the arrangement of secondary structural elements and is more similar to viral helicases such as NS3. The N-terminus of the DHX9 core contains two long alpha-helices that reside on the surface of the core without contributing to nucleotide binding
Q08211
enzymatically active fragment of the JEV NTPase/helicase catalytic domain, recombinant protein, crystal structure determined at 1.8 A resolution, data collection and refinement statistics
P27395
crystals of the recombinant C-terminal helicase domain are obtained by the hanging-drop vapour-diffusion method
-
RNA helicase Hera C-terminal domain, vapour diffusion, microbatch under oil
-
hanging-drop vapor diffusion method, the 1.8 A crystal structure of the helicase region of the YFV NS3 protein (includes residues 187 to 623) and the 2.5 A structure of its complex with ADP
P03314
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
70
-
the enzyme starts to unfold at 20C and fully unfolds at 70C
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant GST-fusion wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by glutathione affinity chromatography
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-, EF409381
using Ni-NTA chromatography
-, Q83DM8
; recombinant His-tagged catalytic domain of the NS3 helicase domain from dengue virus serotype 4 from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration
-
recombinant His-tag C-terminal domain of NS3 protein from Escherichia coli by nickel affinity chromatography; recombinant protein, gel filtration, SDS-PAGE
-
recombinant wild-type and N-terminally truncated enzyme from Escherichia coli
-
recombinant His-tagged wild-type and mutant RhlB and RNaseE from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
gel filtration
Q9WPH5
gel filtration, recombinant nonstructural protein 3
-
gel filtration, recombinant protein
-
gel filtration, SDS-PAGE
-
gel filtration, SDS-PAGE; recombinant His10-tagged Arg-rich amino acid motif HCV1487-1500, complete domain 2, and domain 2 lacking the flexible loop from Escherichia coli strain BL21(DE3)
P27958
recombinant C-terminally His-tagged truncated NS3 NTPase/helicase domain from Escherichia coli by nickel affinity chromatography
-
recombinant enzyme
-
truncated and full-length complexes between nonstructural protein 3 (NS3) and nonstructural protein 4A (NS4), NS3-4A complex purifies as two separable proteins, gel filtration, SDS-PAGE
-
using affinity chromatography
-
using Ni-NTA chromatography; using Ni-NTA chromatography
-
gel filtration, recombinant protein
P27395
recombinant enzyme
-
gel filtration, recombinant protein, soluble form; recombinant soluble His6-tagged C-terminal portion of NS3 in Escherichia coli by nickel affinity chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of GST-fusion wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
-
expression of the N-terminally His-tagged enzyme as soluble protein in Escherichia coli strain BL21(DE3); overexpressed as His-tag fusion protein in Escherichia coli
-, EF409381
expression of wild-type and mutant His-tagged NS3 helicase domain in Escherichia coli
-, Q9YS30
expressed in Escherichia coli as a His-tagged fusion protein
-, Q83DM8
expressed in Escherichia coli, recombinant protein; expression of NS3 ATPase/helicase in Escherichia coli, expression of the His-tag C-terminal domain
-
expression in Escherichia coli; expression of the His-tagged catalytic domain of the NS3 helicase domain from dengue virus serotype 4 in Escherichia coli strain BL21
-
expression of wild-type and N-terminally truncated enzyme in Escherichia coli
-
construction of a di-cistronic vector that overexpresses a complex comprising RhlB and its recognition site within RNase E, corresponding to residues 696-762, the expression construct is termed pRneRhlBDELTA1-397. Expression of His-tagged wild-type and mutant RhlB and RNaseE in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3), recombinant protein, NS3d2wt variant corresponding to wild-type domain 2, NS3d2D construct comprises the complete domain, HCV(1361-1503) without loop, pET21b andpET16b vectors; expression of the Arg-rich amino acid motif HCV1487-1500, of the complete domain 2, and of domain 2 lacking the flexible loop localized between Val1458 and Thr1476 as His10-tagged proteins in Escherichia coli strain BL21(DE3)
P27958
expressed in Escherichia coli, strain Rosetta (DE3), recombinant nonstructural protein 3
-
expressed in Escherichia coli, strains XL-1 Blue, Rosetta (DE3), M15 (pREP4), vector pET-21-2c, kinetics of NS3 protein accumulation upon its expression in Escherichia coli at 25C for 1-5 h shown
-
expression of C-terminally His-tagged truncated NS3 NTPase/helicase domain in Escherichia coli
-
expression of wild-type and mutant NS3, cloning of a His6-tag to the N-terminus of NS3 greatly increases its affinity for RNA; NS3-plus and NS3/4a-plus genes expressed in Escherichia coli, composition of NS3-4A expression product using the pet-SUMO vector
Q9WPH5
NS3-plus and NS3/4a-plus genes expressed in Escherichia coli, generation of NS3-4A expression product, pET15b and pet-SUMO vector
-
expressed in Escherichia coli BL-21
-
expression in Escherichia coli
-
overexpression in Escherichia coli
-
recombinantly expressed as a His-tagged fusion protein; recombinantly expressed as a His-tagged fusion protein
-
expressed in Escherichia coli BL21 (DE3), recombinant protein, pET21b vector
P27395
expression of the C-terminal helicase domain (amino-acid sequence corresponding to that between residues 189 and 620 of the predicted NS3 polypeptide) in Escherichia coli
-
expression of NS3 as maltose-binding protein furion protein using the constitutive elongation factor-1alpha promoter in HEK-293T cells. Plant viral RSS protein NS3 complements HIV-1 Tat based on the sequestration of small dsRNA
-
expression in Escherichia coli
-
C-terminal domain of Hera is overproduced in Escherichia coli
-
baculovirus expression system
P0C6X1
overexpression in Escherichia coli
Q9M6R6, -
expressed in Escherichia coli, C-terminal portion with the ATPase/helicase domain, plasmid pET-30a; expression of the soluble His6-tagged C-terminal portion of NS3 in Escherichia coli C41 cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression is downregulated by high-K+ and stress
-
expression of AtHELPS is induced by low-K+, zeatin and cold treatments
-
an alpha-helix that inserts between the conserved domains of the free protein negatively regulate ATPase activity
Q9UMR2
polymerase II can interact with beta-actin, and this interaction is enhanced due to the overexpression of RNA helicase A
-
GRTH gene expression is transcriptionally upregulated by human chorionic gonadotropin (hCG) via second messenger (cAMP) and androgen in Leydig cells. The expression of GRTH in testicular cells is differentially regulated by its 5' flanking sequence. The 1 kb fragment of GRTH gene (5' to the ATG codon) contains sequences for androgen regulation of its expression in Leydig cells
-
furing development, expression of Supv3L1 begins at the blastocyst stage, becomes widespread and strong in all fetal tissues and cell types, and continues during postnatal growth. Supv3L1 is an developmentally regulated gene, which continues to be expressed in all mature tissues, particularly the rapidly proliferating cells of testes, but also in the brain and sensory organs
Q80YD1
overexpression promotes White Collar-1 accumulation, confirming that FRQ-interacting RNA helicase together with the circadian oscillator component FREQUENCY (FRQ) plays a role in White Collar-1 stabilization
Neurospora sp.
-
crhR is constitutively expressed under light; upon incubation of Synechocystis cells at low temperature, the crhR gene is transiently upregulated and the resultant CrhR protein accumulates in the cytosol
-
cold-inducible RNA helicase; the enzyme is more dominantly transcribed at 60C than at 85C and 93C in both logarithmic and stationary phases. Tk-DeaD is detected only in logarithmic-phase cells cultivated at 60C but hardly detected at 85C and 93C in both phases Tk-DeaD expression is, hence, post-transcriptionally regulated and appears under vigorous growth conditions at 60C
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A115C/D262C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
A115C/E224C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
A115C/S229C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
S108C/E224C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
S108C/S229C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
D755A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 90% reduced ATPase activity compared to the wild-type enzyme
F788A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 30% reduced ATPase activity compared to the wild-type enzyme
G781S
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 75% reduced ATPase activity compared to the wild-type enzyme
H903A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 45% reduced ATPase activity compared to the wild-type enzyme
Q785A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 65% reduced ATPase activity compared to the wild-type enzyme
Q785E
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 75% reduced ATPase activity compared to the wild-type enzyme
R791A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 10% increased ATPase activity compared to the wild-type enzyme
R815L
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 60% increased ATPase activity compared to the wild-type enzyme
R938A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 45% reduced ATPase activity compared to the wild-type enzyme
S790A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 60% reduced ATPase activity compared to the wild-type enzyme
S790W
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 70% reduced ATPase activity compared to the wild-type enzyme
T812A/Y813A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows unaltered ATPase activity compared to the wild-type enzyme
K199A/T200A
-
site-directed mutagenesis, mutant avoid of basal and of RNA-stimulated NTPase activity; site-directed mutagenesis, the mutation in the C-terminal domain of NS3 eliminates both the basal and the RNA-stimulated NTPase activity
H51A
-
site-directed mutagenesis, the mutant has an inactivated protease domain showing enhanced RNA helicase compared to wild-type full-length enzyme
R184Q/K185N/R186G/K187N
-
construction of the N-terminally truncated mutant NS3DELTA180 containing a mutated RNA substrate biding motif, the mutant shows reduced RTPase activity
K199A/T200A
Dengue virus PL046
-
site-directed mutagenesis, mutant avoid of basal and of RNA-stimulated NTPase activity; site-directed mutagenesis, the mutation in the C-terminal domain of NS3 eliminates both the basal and the RNA-stimulated NTPase activity
-
D310H
-
site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview
D313H
-
site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview
H320D
-
site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview
Y383A
-
site-directed mutagenesis, the mutation causes the formation of a higher order molecular weight species in binding of RNaseE by RhlB
H293A
-
mutation results in a protein with a significantly higher level of ATPase in the absence of RNA. The mutant protein still unwinds RNA. In the presence of RNA, the H293A mutant hydrolyzes ATP slower than wild-type
S1369R
Q9WPH5
NS3-4A construct, suppressor mutant, ATP-coupled RNA affinity identical to that of wild-type NS3-4A; site-directed mutagenesis, the NS3-4A mutant shows increased ATPase activity and RNA stimulation activity compared to wild-type NS3
S1369R/M1708A
Q9WPH5
NS3-4A construct, reduced ATP-coupled RNA affinity of the single mutant suppressed by the addition of the S1369R mutation; site-directed mutagenesis, the NS3-4A mutant shows increased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
S1369R/Y1702A
Q9WPH5
NS3-4A construct, reduced ATP-coupled RNA affinity of the single mutant suppressed by the addition of the S1369R mutation; site-directed mutagenesis, the NS3-4A mutant shows decreased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
Y1702A
Q9WPH5
NS3-4A construct, ability to bind and unwind RNA in vitro, mutation reduces functional NS3-4A binding affinity for RNA by 500-fold relative to the wild-type; site-directed mutagenesis, the NS3-4A mutant shows decreased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
DELTA53-105
-
a region within the N-terminus of RHAU, referred to as the RSM, interacts with human telomerase RNA
K236E
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K54A/K55A
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
Y593F
-
expression of the mutant enzyme in SW620 cells leads to Snail repression, E-cadherin upregulation and vimentin repression
G199A
P27395
mutation in WALKER A motif, PCR-based mutagenesis, ATPase and RNA helicase activity lost
G460A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
G463A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
K200A
P27395
mutation in WALKER A motif, PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200D
P27395
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200E
P27395
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200H
P27395
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200N
P27395
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200Q
P27395
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200R
P27395
PCR-based mutagenesis, ATPase and RNA helicase activity lost
Q457A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, 80% reduction of ATPase activity, no RNA helicase activity
R458A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, 90% reduction of ATPase activity, no RNA helicase activity
R459A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
R461A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no ATPase activity, no RNA helicase activity
R464A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no ATPase activity, no RNA helicase activity
T201A
P27395
mutation in WALKER A motif, PCR-based mutagenesis, ATPase and RNA helicase activity lost
V462A
P27395
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
F162A
-
kcat/KM for ATP is 1% of wild-type value
F162L
-
kcat/KM for ATP is 25% of wild-type value
K177A
P47047
mutant enzyme shows no stimulation of ATPase activity by single-stranded RNA
Q169A
-
kcat/KM for ATP is 0.3% of wild-type value
Q169E
-
kcat/KM for ATP is 0.4% of wild-type value
T166A
-
kcat/KM for ATP is 37% of wild-type value
T166S
-
kcat/KM for ATP is 26% of wild-type value
E300A
-
mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
H299A
-
mutation elicits defects in RNA unwinding but spares the ATPase activity
K191A
-
mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
R229A
-
mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
T192A
-
mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
T326A
-
mutation elicits defects in RNA unwinding but spares the ATPase activity
T328A
-
mutation elicits defects in RNA unwinding but spares the ATPase activity
D172A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 41% of the ratio determined for the wild-type enzyme
E169A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 38% of the ratio determined for the wild-type enzyme
E173A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 17% of the ratio determined for the wild-type enzyme
E180A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 35% of the ratio determined for the wild-type enzyme
E182A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 29% of the ratio determined for the wild-type enzyme
F179A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 19% of the ratio determined for the wild-type enzyme
K186A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 15% of the ratio determined for the wild-type enzyme
K187A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 8% of the ratio determined for the wild-type enzyme
Q188A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 33% of the ratio determined for the wild-type enzyme
R170A
-
the ration of (kcat/Km)ATP/(kcat/Km)GTP is 31% of the ratio determined for the wild-type enzyme
R185A
-
inactive mutant enzyme
K691A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 80% reduced ATPase activity compared to the wild-type enzyme
additional information
-
trans interference by BMV 1a protein helicase mutants with BMV 1a protein-stimulated RNA3 accumulation, overview
K232A
-, Q9YS30
site-directed mutagenesis in the helicase domain of NS3
additional information
-, Q9YS30
for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B
K232A
Classical swine fever virus CSFV
-
site-directed mutagenesis in the helicase domain of NS3
-
additional information
Classical swine fever virus CSFV
-
for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B
-
M1708A
Q9WPH5
NS3-4A construct, ability to bind and unwind RNA in vitro, mutation reduces functional NS3-4A binding affinity for RNA by 500-fold relative to the wild-type; site-directed mutagenesis, the NS3-4A mutant shows decreased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
additional information
Q9WPH5
construction of the NS3-4A mutant affected in its acidic domain, the mutant shows altered RNA binding and increased ATPase activity, kinetics, overview
K54A/K55A/K236E
-
triple mutant shows a severe reduction in interaction with junD post-transcriptional control element (PCE) or SNV PCE compared with wild-type
additional information
P26196
mutagenesis of conserved p54 helicase motifs activates translation in the tethered function assay, reduces accumulation of p54 in P-bodies in HeLa cells, and inhibits its capacity to assemble P-bodies in p54-depleted cells
additional information
-
recombinant RHA domains are evaluated for binding activity to post-transcriptional control element (PCE) in comparison with nonfunctional PCE and generic control double-stranded RNAs (dsRNAs). N-terminal domain exhibits higher binding affinity for PCE than for nonfunctional mutant RNA or control dsRNA. Highly conserved surface-exposed lysine residues are required for selective interaction with PCE RNA. In cells, the N-terminal domain directs interaction with PCE, mRNA and its exogenous expression blocks the translation activity of endogenous RHA
R806H
Neurospora sp.
-
interacts with the circadian oscillator component FREQUENCY (FRQ), but interaction between the FRQFRHR806H complex (FFC) and White Collar Complex is severely affected
additional information
-
the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions. Point mutations in a single conserved basic amino acid residue upstream of motif I have little effect on the activities of C-terminally truncated mutants of both TGBp1 proteins. When introduced into the full-length NTPase/helicase domains, these mutations cause a substantial decrease in the ATPase activity of the protein, suggesting that the conserved basic amino acid residue upstream of motif I is required to maintain a reaction-competent conformation of the TGBp1 ATPase active site
additional information
-
an NS3 mutant, that is deficient in RNA binding and its associated RSS activity, is inactive in complementing the RNA silencing suppressor function of the Tat protein of Human immunodeficiency virus type 1
additional information
Rice hoja blanca virus RHBV
-
an NS3 mutant, that is deficient in RNA binding and its associated RSS activity, is inactive in complementing the RNA silencing suppressor function of the Tat protein of Human immunodeficiency virus type 1
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
the enzyme is a target for development of specific antiviral inhibitors
drug development
-
the multifunctional NS3 protein from Dengue virus is a target for the design of antiviral inhibitors
drug development
-
the enzyme is a target for anti-HCV drug development
pharmacology
-
peptide inhibitors reproducing the structure of the autoregulatory motif as possibility to develop effective antivirals
medicine
O15523, Q9NQI0
DDX4 can serve as a useful and highly specific biomarker for the diagnosis of germ cell tumors; DDX4 can serve as a useful and highly specific biomarker for the diagnosis of germ cell tumors
medicine
-
mutation within hBrr2p can be linked to autosomal dominant retinitis pigmentosa
pharmacology
P27395
conservation of the NTP-binding pocket among viruses of the family Flaviviridae as potential for development of therapeutics
medicine
Q501J6, Q61656, Q9QY15
DDX4 can serve as a useful and highly specific biomarker for the diagnosis of germ cell tumors; DDX4 can serve as a useful and highly specific biomarker for the diagnosis of germ cell tumors; DDX4 can serve as a useful and highly specific biomarker for the diagnosis of germ cell tumors
medicine
Q9QY16
DDX4 can serve as a useful and highly specific biomarker for the diagnosis of germ cell tumors