3.5.4.37: double-stranded RNA adenine deaminase
This is an abbreviated version!
For detailed information about double-stranded RNA adenine deaminase, go to the full flat file.
Word Map on EC 3.5.4.37
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3.5.4.37
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inosine
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a-to-i
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deaminases
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deamination
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adenosine-to-inosine
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hereditaria
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rna-editing
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pre-mrnas
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dyschromatosis
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symmetrica
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z-dna
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duplex
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ampa
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left-handed
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unedited
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glur-b
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recoding
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site-selective
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macules
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interferon-inducible
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mda5
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hypopigmented
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ifn-inducible
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dsrbds
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interferon-stimulated
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ca2+-permeable
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5-ht2cr
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dicer
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samhd1
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genodermatosis
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rig-i
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hypermutation
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ifn-stimulated
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pigmentary
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interferonopathy
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autoinflammatory
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medicine
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inosine-containing
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dsrna-binding
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drug development
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protein-rna
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antigenome
- 3.5.4.37
- inosine
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a-to-i
- deaminases
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deamination
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adenosine-to-inosine
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hereditaria
-
rna-editing
- pre-mrnas
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dyschromatosis
-
symmetrica
- z-dna
- duplex
- ampa
-
left-handed
-
unedited
-
glur-b
-
recoding
-
site-selective
-
macules
-
interferon-inducible
- mda5
-
hypopigmented
-
ifn-inducible
-
dsrbds
-
interferon-stimulated
-
ca2+-permeable
-
5-ht2cr
- dicer
- samhd1
-
genodermatosis
- rig-i
-
hypermutation
-
ifn-stimulated
-
pigmentary
-
interferonopathy
-
autoinflammatory
- medicine
-
inosine-containing
-
dsrna-binding
- drug development
-
protein-rna
-
antigenome
Reaction
Synonyms
ADAR, ADAR1, ADAR1L, ADAR1S, ADAR2, ADAR2 deaminase, adenosine deaminase acting on RNA 1, adenosine deaminase acting on RNA-1, APOBEC1, bADAR1a, CiADAR1, dADAR, double-stranded RNA adenosine deaminase, double-stranded RNA-specific adenosine deaminase, double-stranded RNA-specific adenosine deaminase 1, double-stranded-RNA-specific adenosine deaminase 1, DRADA1, dsRAD, dsRNA adenosine deaminase, hADAR1, hADAR1a, hADAR2, hADAR2-D
ECTree
3.5.4.37 double-stranded RNA adenine deaminaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.4.37 - double-stranded RNA adenine deaminase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-azaadenine in double-stranded RNA + H2O
8-azahypoxanthine in double-stranded RNA + NH3
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8-aza substitution at adenosine in various RNA substrates accelerates the rate of deamination at these sites by ADAR2 (2.8-17-fold). The magnitude of this effect depends on the RNA structural context of the reacting nucleotide
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-
?
adenosine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
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-
?
N6-methyladenine in double-stranded RNA + H2O
N6-methylhypoxanthine in double-stranded RNA + NH3
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slow substrate for ADAR2, 2% of the rate compared to that of adenosine
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
identification of ADAR substrates. RNA hairpins in noncoding regions of Caenorhabditis elegans mRNA are edited
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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A-to-I editing is a form of nucleotide substitution editing, because I is decoded as guanosine instead of A by ribosomes during translation and by polymerases during RNA-dependent RNA replication. Additionally, A-to-I editing can alter RNA structure stability as I:U mismatches are less stable than A:U base pairs. Both viral and cellular RNAs are edited by ADARs. A-to-I editing is of broad physiologic significance. Among the outcomes of A-to-I editing are biochemical changes that affect how viruses interact with their hosts, changes that can lead to either enhanced or reduced virus growth and persistence depending upon the specific virus
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 has the potential both to change information content through editing of mRNA and to regulate gene expression through interacting with the NF90 family proteins
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 is an editing enzyme that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR2 is an editing enzymes that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. The enzyme functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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editing of RNA changes the read-out of information from DNA by altering the nucleotide sequence of a transcript. One type of RNA editing found in all metazoans uses double-stranded RNA (dsRNA) as a substrate and results in the deamination of adenosine to give inosine, which is translated as guanosine
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
the enzyme catalyzes the hydrolytic deamination of adenosine to inosine in completely or partially double-stranded RNA
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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ADAR1 contains a domain (Zalpha) that binds specifically to the left-handed Z-DNA conformation with high affinity. As formation of Z-DNA in vivo occurs 5' to, or behind, a moving RNA polymerase during transcription, recognition of Z-DNA by DRADA1 provides a plausible mechanism by which DRADA1 can be targeted to a nascent RNA so that editing occurs before splicing
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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ADAR1-S edits HDV RNA during replication
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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identification of ADAR substrates. RNA hairpins in noncoding regions of human brain mRNA are edited
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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like ADAR1, ADAR2 has a 5' neighbor preference (A = U > C = G), but, unlike ADAR1, also has a 3' neighbor preference (U = G > C = A). ADAR2 prefers certain trinucleotide sequences (UAU, AAG, UAG, AAU). ADAR1 and ADAR2 have overlapping specificities. Xenopus and human ADAR1 have a highly similar, or identical, deamination specificity
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
RNA editing catalyzed by ADAR1 and ADAR2 involves the site-specific conversion of adenosine to inosine within imperfectly duplexed RNA. ADAR1- and ADAR2-mediated editing occurs within transcripts of glutamate receptors in the brain and in hepatitis delta virus RNA in the liver. The Q/R site within the GluR-B premessage is edited more efficiently by ADAR2 than it is by ADAR1. The converse is true for the 160 site within this same transcript. The base-pairing status of the targeted adenosine can affect the efficiency of editing by both ADAR1 and ADAR2. When the the substrate contains an A:C mismatch at the editing site, editing by both ADARs is enhanced compared to when A:A or A:G mismatches or A:U base pairs occurr at the same site. The deaminase domains plays a dominant role in defining the substrate specificity of the resulting enzyme
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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the specificity of the ADAR1 and ADAR2 deaminases ranges from highly site-selective to non-selective, dependent on the duplex structure of the substrate RNA
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 has a preference for binding simple duplex RNA as compared to highly structured RNA substrates
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
the nucleoside analog 8-azanebularine is introduced into this RNA (and derived constructs) to mechanistically trap the protein-RNA complex without catalytic turnover for EMSA and ribonuclease footprinting analyses. The human ADAR2 deaminase domain requires duplex RNA and is sensitive to 2-deoxy substitution at nucleotides opposite the editing site, the local sequence and 8-azanebularine nucleotide positioning on the duplex. The human ADAR2 deaminase domain protects about 23 nt on the edited strand around the editing site in an asymmetric fashion (about 18 nt on the 5' side and about 5 nt on the 3x02 side)
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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editing of Blcap, FlnA, and some sites within B1 and B2 SINEs clearly depends on ADAR1
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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ADAR1 specifically or preferentially edits 5HT2CR A and B sites
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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the enzyme is involved in involved in the editing of mammalian RNAs by the site-specific conversion of adenosine to inosine
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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editing frequency in rADAR2 pre-mRNA. Both sequence and structural elements are required to define adenosine moieties targeted for specific ADAR2-mediated deamination
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
pre-mRNA of glutamate receptor subunit B. ADAR2 selectively edits the R/G site (R/G stem-loop), while ADAR1 edits more promiscuously at several other adenosines in the double-stranded stem. The immediate structure surrounding the editing site is important. A purine opposite to the editing site has a negative effect on both selectivity and efficiency of editing. More distant internal loops in the substrate have minor effects on site selectivity, while efficiency of editing is influenced. Changes in the RNA structure that affected editing do not alter the binding abilities of ADAR2. Binding and catalysis are independent events
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-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
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dsRNA is deaminated at the same sites whether it exists as a free molecule or is flanked by internal loops. Internal loops delineate helix ends for ADAR1. Since ADAR1 deaminates short RNAs at fewer adenosines than long RNAs, loops decrease the number of deaminations within an RNA by dividing a long RNA into shorter substrates
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-
?
additional information
?
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overexpression of p150 ADAR1 has no significant effect on the yield of vesicular stomatitis virus. reduction of p110 and p150 ADAR1 proteins to less than 10% to 15% of parental levels (ADAR1-deficient) has no significant effect on growth of Vesicular Stomatitis Virus in the absence of interferon treatment. The level of phosphorylated protein kinase PKR is increased in ADAR1-deficient cells compared to ADAR1-sufficient cells following IFN treatment, regardless of viral infection. ADAR1 suppresses activation of protein kinase PKR and inhibition of growth of Vesicular Stomatitis Virus in response to interferon treatment
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-
?
additional information
?
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human APOBEC1 possesses no antiviral activity
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-
?
additional information
?
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-
no product is observed with N6-ethyladenosine or 2,6-diaminopurine ribonucleoside in double-stranded RNA
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-
?
