5.4.99.B22: multisite-specific tRNA pseudouridine synthase
This is an abbreviated version!
For detailed information about multisite-specific tRNA pseudouridine synthase, go to the full flat file.
Word Map on EC 5.4.99.B22
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5.4.99.B22
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pseudouridylation
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anemia
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sideroblastic
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myopathy
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dyskerin
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anticodon
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mlasa
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spliceosomal
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nuclear-encoded
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agriculture
- 5.4.99.B22
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pseudouridylation
- anemia
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sideroblastic
- myopathy
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dyskerin
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anticodon
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mlasa
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spliceosomal
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nuclear-encoded
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Reaction
Synonyms
cePus1p, dmPus1p, hPus1p, mPus1p, pseudouridine synthase 1, pseudouridine synthase Pus10, PUS1, Pus1p, Pus4, PUS6, PUS7, RluE, RNA:pseudouridine synthases 1, RPUSD4, scPus1p, spPus1p, SVR1, TgPUS1, xtPus1p, YmfC
ECTree
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Substrates Products
Substrates Products on EC 5.4.99.B22 - multisite-specific tRNA pseudouridine synthase
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REACTION DIAGRAM
human pre-tRNASer(UGA) uridine27
human pre-tRNASer(UGA) pseudouridine27
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mitochondrial tRNAPhe uridine39
mitochondrial tRNAPhe pseudouridine39
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yeast pre-tRNAIle uridine
yeast pre-tRNAIle pseudouridine
possible modification sites are uridine 27, uridine30, uridine34 or uridine36
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23S rRNA pseudouridine2457
RluE forms a highly conserved pseudouridine during ribosome biogenesis
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23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE recognizes a large part of 23S rRNA comprising both H89 and the single-stranded flanking regions which explains the high substrate specificity of RluE
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23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE forms a highly conserved pseudouridine during ribosome biogenesis
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KAR2 mRNA pseudouridine
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KAR2 mRNA uridine
KAR2 mRNA pseudouridine
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RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
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RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
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TEF1 mRNA pseudouridine239
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TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
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tRNAArg(ACG) pseudouridine1
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Pus1p can catalyze pseudouridine1 formation in the mature tRNAArg, the pre-tRNAArg, and its maturation intermediates
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tRNAArg(ACG) uridine1
tRNAArg(ACG) pseudouridine1
Pus1p can catalyze pseudouridine1 formation in the mature tRNAArg, the pre-tRNAArg, and its maturation intermediates
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tRNAIle(UAU) pseudouridine27
intron-independent reaction
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tRNAIle(UAU) uridine27
tRNAIle(UAU) pseudouridine27
intron-independent reaction, reaction is catalyzed efficiently
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tRNAIle(UAU) pseudouridine34
intron-dependent reaction
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tRNAIle(UAU) uridine34
tRNAIle(UAU) pseudouridine34
reaction is strictly intron-dependent
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tRNAIle(UAU) pseudouridine36
intron-dependent reaction
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tRNAIle(UAU) uridine36
tRNAIle(UAU) pseudouridine36
reaction is strictly intron-dependent
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Pus1p from Caenorhabditis elegans has no enzymatic activity on U2 snRNA when expressed in yeast cells. Substrate specificity analysis and comparison of different species
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additional information
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
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additional information
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
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additional information
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Pus1p modifies uridines at positions 1, 26, 27, 28, 30, 34, 36, 65, and 67 depending on the source of the enzyme (Saccharomyces cerevisiae or mouse), the substrates (intron-containing or not), or whether the activity is monitored in vivo or in vitro. Out of all the positions that Pus1p modifies, the modification of uridines at positions 27 and 28 is by far the most common in tRNAs, with pseudouridine infrequently found at the other positions that the Pus1p enzymes recognize
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additional information
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Pus1p modifies uridines at positions 1, 26, 27, 28, 30, 34, 36, 65, and 67 depending on the source of the enzyme (Saccharomyces cerevisiae or mouse), the substrates (intron-containing or not), or whether the activity is monitored in vivo or in vitro. Out of all the positions that Pus1p modifies, the modification of uridines at positions 27 and 28 is by far the most common in tRNAs, with pseudouridine infrequently found at the other positions that the Pus1p enzymes recognize
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additional information
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pseudouridine synthase assays of hPus1p enzymes tRNA and HP7 SRA RNA substrates, i.e. RNA of the minimal RNA fragment within steroid receptor RNA activator (SRA), termed HP7. Mouse mitochondrial tRNAAsp is used as a positive control for hPus1p activity
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additional information
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pseudouridine synthase assays of hPus1p enzymes tRNA and HP7 SRA RNA substrates, i.e. RNA of the minimal RNA fragment within steroid receptor RNA activator (SRA), termed HP7. Mouse mitochondrial tRNAAsp is used as a positive control for hPus1p activity
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additional information
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. In vertrbrates, SCARNA8 (also known as U92 scaRNA) is a guide for U2-Psi43 in addition to established targets U2-Psi34/Psi44. U2 snRNA is identified as a genuine substrate for mPus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-Psi43 (or 44) in yeasts, Drosophila, and vertebrates
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additional information
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Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
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additional information
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Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
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additional information
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Pus1 from Saccharomyces cerevisiae is a multisite-specific enzyme that catalyses the formation of pseudouridine residues at different positions in several tRNA transcripts
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additional information
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for tRNA and Pus7, many known sites and their associated modifiers are identified, including Pus1-mediated Psi sites at positions 26-28 in several tRNAs, Pus7-dependent sites at position 13 of glutamate tRNA, Pus9-dependent site in mitochondrial aspartate tRNA at position 32, and Deg1-dependent sites at positions 37-38 in several tRNAs. Pseudouridylation in ncRNAs at sites of inter or intra-molecular interactions
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additional information
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Pus1p is the only pseudouridine synthase in Saccharomyces cerevisiae that is active on U2 snRNA at position 44. Yeast U2 snRNA is normally pseudouridylated at positions 35, 42, and 44
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additional information
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Besides U2 and U6 snRNAs in Saccharomyces cerevisiae, the enzyme modifies uridines in many different tRNAs. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
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additional information
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Pus1p is the only pseudouridine synthase in Saccharomyces cerevisiae that is active on U2 snRNA at position 44. Yeast U2 snRNA is normally pseudouridylated at positions 35, 42, and 44
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?
additional information
?
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Besides U2 and U6 snRNAs in Saccharomyces cerevisiae, the enzyme modifies uridines in many different tRNAs. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
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-
?
additional information
?
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-Psi43 (or 44) in yeasts, Drosophila, and vertebrates
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-
?
additional information
?
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-Psi43 (or 44) in yeasts, Drosophila, and vertebrates
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?
additional information
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extensive, regulated pseudouridylation of Toxoplasma mRNA with evidence for 1669 and 394 sites of pseudouridylation in tachyzoite and bradyzoite mRNAs, respectively. The distribution of Us and Psis is significantly different between the three regions of the transcript. Pseudouridylation is underrepresented in the 3'-UTR. At least in tachyzoites, TgPUS1-dependent Psis are distributed within the codon comparably toTgPUS1-independent Psis
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additional information
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extensive, regulated pseudouridylation of Toxoplasma mRNA with evidence for 1669 and 394 sites of pseudouridylation in tachyzoite and bradyzoite mRNAs, respectively. The distribution of Us and Psis is significantly different between the three regions of the transcript. Pseudouridylation is underrepresented in the 3'-UTR. At least in tachyzoites, TgPUS1-dependent Psis are distributed within the codon comparably toTgPUS1-independent Psis
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additional information
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identification of TgPUS1-dependent Psis in Toxoplasma RNA. Psis are relatively depleted in the 3'-UTR but enriched at position 1 of codons, identification by CMCT treatment combined with deep sequencing. Human rRNA data can be used to establish criteria for identification of Psis with high confidence, method evaluation, overview. PSI-seq identifies evolutionarily conserved sites of pseudouridylation in Toxoplasma gondii rRNAs. Determination of three TgPUS1-dependent Psis, all in the 5' half of the anticodon arm, specifically at positions 27 and 34 of tRNA Val and Asn (TGME49_251700 and TGME49_293750) in tachyzoites and position 28 of tRNA Ile (TGME49_262568) in bradyzoites
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additional information
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identification of TgPUS1-dependent Psis in Toxoplasma RNA. Psis are relatively depleted in the 3'-UTR but enriched at position 1 of codons, identification by CMCT treatment combined with deep sequencing. Human rRNA data can be used to establish criteria for identification of Psis with high confidence, method evaluation, overview. PSI-seq identifies evolutionarily conserved sites of pseudouridylation in Toxoplasma gondii rRNAs. Determination of three TgPUS1-dependent Psis, all in the 5' half of the anticodon arm, specifically at positions 27 and 34 of tRNA Val and Asn (TGME49_251700 and TGME49_293750) in tachyzoites and position 28 of tRNA Ile (TGME49_262568) in bradyzoites
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additional information
?
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dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. In vertrbrates, SCARNA8 (also known as U92 scaRNA) is a guide for U2-Psi43 in addition to established targets U2-Psi34/Psi44. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
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?