3.1.13.B1: 5'-3' exoribonuclease
This is an abbreviated version!
For detailed information about 5'-3' exoribonuclease, go to the full flat file.
Word Map on EC 3.1.13.B1
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3.1.13.B1
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decapping
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sfrnas
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deadenylation
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flaviviruses
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exonucleolytic
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pyrophosphohydrolase
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exoribonucleolytic
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p-bodies
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pre-rrnas
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pacman
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flaviviral
- 3.1.13.B1
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decapping
-
sfrnas
-
deadenylation
- flaviviruses
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exonucleolytic
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pyrophosphohydrolase
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exoribonucleolytic
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p-bodies
- pre-rrnas
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pacman
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flaviviral
Reaction
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates =
Synonyms
5'-3' exoribonuclease 2, 5'-to-3' exoribonuclease, Pab-RNase J, PAB1751, Rat1, Saci-aCPSF2, Saci2362, Sso-RNase J, SSO0386, Tk-RNase J, Tk1469
ECTree
3.1.13.B1 5'-3' exoribonucleaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.1.13.B1 - 5'-3' exoribonuclease
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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
(A)40 + 38 H2O
adenosine + 39 AMP
(A)40 is a 40-nt-long synthetic RNA harboring a single radioactively labeled A nucleotide at the 5'-end. When compared with the triphosphorylated RNA, SSSO-RNase J displayes a twofold higher velocity in degrading mono-phosphorylated RNA and RNA bearing a 5'-hydroxyl group
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-
?
(A)40 + 38 H2O
adenosine + 39 AMP
(A)40 is a 40-nt-long synthetic RNA harboring a single radioactively labeled A nucleotide at the 5'-end. When compared with the triphosphorylated RNA, SSSO-RNase J displayes a twofold higher velocity in degrading mono-phosphorylated RNA and RNA bearing a 5'-hydroxyl group
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-
?
5'-pA(A)39 + H2O
40 AMP
5'-pA(A)39 is a 40-nt-long synthetic RNA harboring a 5'-monophosphate and a single radioactively labeled A nucleotide at the 5'-end. When compared with the triphosphorylated RNA, the enzyme displayes a twofold higher velocity in degrading mono-phosphorylated RNA and RNA bearing a 5'-hydroxyl group
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-
?
5'-pA(A)39 + H2O
40 AMP
5'-pA(A)39 is a 40-nt-long synthetic RNA harboring a 5'-monophosphate and a single radioactively labeled A nucleotide at the 5'-end. When compared with the triphosphorylated RNA, the enzyme displayes a twofold higher velocity in degrading mono-phosphorylated RNA and RNA bearing a 5'-hydroxyl group
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-
?
5'-pC-sR47 + H2O
5'-phosphomononucleotides
sR47 RNA labeled either at its 5' end as a 5'-[32P]monophosphate. The enzyme is a highly processive 5'-to-3'-exoribonuclease.The principal product of the 5' end-labeled RNA is [32P]GMP as guanosine is the 5'-nucleotide of sR47. Single-stranded DNA is degraded by the enzyme, suggesting that the it does not discriminate between ribose and 2'-deoxyribose nucleosides. Double-stranded DNA is resistant to degradation. The enzyme requires a free 5' end to initiate degradation
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-
?
5'-pC-sR47 + H2O
5'-phosphomononucleotides
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
sR47 RNA labeled either at its 5' end as a 5'-[32P]monophosphate. The enzyme is a highly processive 5'-to-3'-exoribonuclease.The principal product of the 5' end-labeled RNA is [32P]GMP as guanosine is the 5'-nucleotide of sR47. Single-stranded DNA is degraded by the enzyme, suggesting that the it does not discriminate between ribose and 2'-deoxyribose nucleosides. Double-stranded DNA is resistant to degradation. The enzyme requires a free 5' end to initiate degradation
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-
?
5'-pppA(A)39 + H2O
ATP + 39 AMP
5'-pppA(A)39 is a 40-nt-long synthetic RNA harboring a 5'-triphosphate and a single radioactively labeled A nucleotide at the 5'-end. When compared with the triphosphorylated RNA, the enzyme displayes a twofold higher velocity in degrading mono-phosphorylated RNA and RNA bearing a 5'-hydroxyl group
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-
?
5'-pppA(A)39 + H2O
ATP + 39 AMP
5'-pppA(A)39 is a 40-nt-long synthetic RNA harboring a 5'-triphosphate and a single radioactively labeled A nucleotide at the 5'-end. When compared with the triphosphorylated RNA, the enzyme displayes a twofold higher velocity in degrading mono-phosphorylated RNA and RNA bearing a 5'-hydroxyl group
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-
?
5'-pppA(A)41 + H2O
ATP + 41 AMP
5'-pppA(A)41 is a 42-nt-long synthetic RNA harboring a 5'-tri-phosphate and a single radioactively labeled A nucleotide at the 5'-end. Decay of 5'-PPP-40A1 RNA results in either a single nucleotide or short oligoribonucleotides, indicating an exoribonucleolytic activity. Degradation with 5' to 3' directionality in vitro
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-
?
5'-pppA(A)41 + H2O
ATP + 41 AMP
5'-pppA(A)41 is a 42-nt-long synthetic RNA harboring a 5'-tri-phosphate and a single radioactively labeled A nucleotide at the 5'-end. Decay of 5'-PPP-40A1 RNA results in either a single nucleotide or short oligoribonucleotides, indicating an exoribonucleolytic activity. Degradation with 5' to 3' directionality in vitro
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-
?
RNA + H2O
3'-phosphomononucleotides
the translation initiation factor a/eIF2(g) binds to the 5'-tri-phosphate terminus of mRNA to protect from 5'-to-3' directional decay and counteract the activity of Sso-RNase J
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?
RNA + H2O
3'-phosphomononucleotides
the translation initiation factor a/eIF2(g) binds to the 5'-tri-phosphate terminus of mRNA to protect from 5'-to-3' directional decay and counteract the activity of Sso-RNase J
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?
RNA + H2O
3'-phosphomononucleotides
the enzyme plays a major role in mRNA turnover
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?
RNA + H2O
3'-phosphomononucleotides
the enzyme plays a major role in mRNA turnover
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?
RNA + H2O
3'-phosphomononucleotides
highly processive 5'-to-3'-exoribonuclease
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?
additional information
?
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Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
pre-tRNA(Trp) is a poor substrate
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?
additional information
?
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using synthetic RNAs as well as 5'-end-labeled natural mRNAs from Sulfolobus solfataricus, no hints for an endonucleolytic activity are obtained
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?
additional information
?
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using synthetic RNAs as well as 5'-end-labeled natural mRNAs from Sulfolobus solfataricus, no hints for an endonucleolytic activity are obtained
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?
additional information
?
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using synthetic RNAs as well as 5'-end-labeled natural mRNAs from Sulfolobus solfataricus, no hints for an endonucleolytic activity are obtained
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?
additional information
?
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nuclear yeast Rat1 catalyzes exonucleolytic cleavage of RNA in the 5'- to 3'-direction to yield nucleoside 5'-phosphates, it forms a complex with Rai1 that stabilizes Rat1 and helps target 5x02 monophosphate RNA by its diphosphohydrolase activity. The efficiency of termination increases as the RNA transcript undergoing degradation by Rat1 gets longer, which suggests that Rat1 may generate a driving force for dissociating RNAPII from the template while degrading the nascent transcripts to catch up to the polymerase. Rat1/Rai1 itself is not sufficient to terminate RNAPII in vitro. Yeast Rat1/Rai1 does not terminate Escherichia coli RNAP, implying that a specific interaction between Rat1/Rai1 and RNAPII may be required for termination. Rat1/Rai1 do not show ATPase activity, ATP hydrolysis may be crucial to promote RNAPII termination but is not driven by Rat1/Rai1. The 5'-3' exoribonuclease activity of Rat1 is essential for RNAPII termination, quantification of the remaining RNAs after Rat1/Rai1 treatment without or with ATP
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?
additional information
?
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nuclear yeast Rat1 catalyzes exonucleolytic cleavage of RNA in the 5'- to 3'-direction to yield nucleoside 5'-phosphates, it forms a complex with Rai1 that stabilizes Rat1 and helps target 5x02 monophosphate RNA by its diphosphohydrolase activity. The efficiency of termination increases as the RNA transcript undergoing degradation by Rat1 gets longer, which suggests that Rat1 may generate a driving force for dissociating RNAPII from the template while degrading the nascent transcripts to catch up to the polymerase. Rat1/Rai1 itself is not sufficient to terminate RNAPII in vitro. Yeast Rat1/Rai1 does not terminate Escherichia coli RNAP, implying that a specific interaction between Rat1/Rai1 and RNAPII may be required for termination. Rat1/Rai1 do not show ATPase activity, ATP hydrolysis may be crucial to promote RNAPII termination but is not driven by Rat1/Rai1. The 5'-3' exoribonuclease activity of Rat1 is essential for RNAPII termination, quantification of the remaining RNAs after Rat1/Rai1 treatment without or with ATP
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?
