3.1.12.1: 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
This is an abbreviated version!
For detailed information about 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming), go to the full flat file.
Reaction
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates =
Synonyms
5' to 3' single stranded DNA exonuclease, BH0340, Cas4, Cas4 nuclease, Cas4-1, Cas4-2, casC, CRISPR adaptation factor, CRISPR-associated Cas4 nuclease, CRISPR-associated exonuclease Cas4, CRISPR-associated protein 4, DUF83Pc, DUF83Ss, Pcal_0546, PF1119, PF1793, SSO0001, TTV1 nucleocapsid protein TP1, type I-C Cas4
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Substrates Products
Substrates Products on EC 3.1.12.1 - 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
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REACTION DIAGRAM
nucleoside 3'-phosphate + ?
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?
single-stranded oligodeoxyribonucleotide + H2O
nucleoside 3'-phosphate + ?
cleavage of a 15T DNA oligonucleotide is observed in the presence of either magnesium or manganese, yielding a cluster of products of around 15 nt in size. A 20U RNA oligonucleotide is cleaved in the presence of manganese but not magnesium.
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?
single-stranded oligodeoxyribonucleotide + H2O
nucleoside 3'-phosphate + ?
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?
single-stranded oligodeoxyribonucleotide + H2O
nucleoside 3'-phosphate + ?
cleavage of a 15T DNA oligonucleotide is observed in the presence of either magnesium or manganese, yielding a cluster of products of around 15 nt in size. A 20U RNA oligonucleotide is cleaved in the presence of manganese but not magnesium.
-
-
?
nucleoside 3'-phosphate + ?
short oligonucleotides (17 nt) are cleaved faster than longer substrates (62 nt). Lack of significant sequence preference toward the substrates containing the Sulfolobus solfataricus protospacer adjacent motif (PAMs) in DNA binding and cleavage reactions in vitro. The rates of cleavage of ssRNA and dsDNA with blunt ends by the enzyme are approximately 20 times and 200 times lower, respectively compared to ssDNA
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-
?
ssDNA + H2O
nucleoside 3'-phosphate + ?
the enzyme is specific for ssDNA
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?
ssDNA + H2O
nucleoside 3'-phosphate + ?
short oligonucleotides (17 nt) are cleaved faster than longer substrates (62 nt). Lack of significant sequence preference toward the substrates containing the Sulfolobus solfataricus protospacer adjacent motif (PAMs) in DNA binding and cleavage reactions in vitro. The rates of cleavage of ssRNA and dsDNA with blunt ends by the enzyme are approximately 20 times and 200 times lower, respectively compared to ssDNA
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?
ssDNA + H2O
nucleoside 3'-phosphate + ?
the enzyme is specific for ssDNA
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?
?
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Cas4 proteins contain a RecB-like nuclease domain and exhibit in vitro exonuclease activities
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?
additional information
?
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Halalkalibacterium halodurans
Cas4 is a Cas1-Cas2-dependent endonuclease that cleaves 3' overhangs of prespacers. Cas4 cleavage is sequence and site-specific and depends on the presence of a protospacer adjacent motif (PAM). Cas4 enhances prespacer processing. Mechanism and structural and mechanistic model, overview
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?
additional information
?
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Halalkalibacterium halodurans
Cas4 proteins contain a RecB-like nuclease domain and exhibit in vitro exonuclease activities. In the presence of Cas1 and Cas2, Cas4 of Bacillus halodurans endonucleolytically cuts long 3' overhangs of prespacers at the PAM site
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?
additional information
?
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Halalkalibacterium halodurans
in the presence of Cas1 and Cas2, Cas4 processes double-stranded substrates with long 3' overhangs through site-specific endonucleolytic cleavage. Cas4 recognizes PAM sequences within the prespacer and prevents integration of unprocessed prespacers, ensuring that only functional spacers will be integrated into the CRISPR array. Assays with dsDNA substrates containing blunt ends or a 24-bp duplex flanked by 15-nt 3' or 5' overhangs result in cleavage of the 3'-overhanging substrates at 65°C, but no cleavage of 5'-overhanging or blunt-end substrates by the enzyme under similar conditions. Exonucleolytic cleavage of the blunt-end substrate is observed using free Cas4, but only at very high concentrations. Sequence-specific integration and asymmetric prespacer processing by the adaptation complex
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?
additional information
?
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Halalkalibacterium halodurans ATCC BAA-125
Cas4 is a Cas1-Cas2-dependent endonuclease that cleaves 3' overhangs of prespacers. Cas4 cleavage is sequence and site-specific and depends on the presence of a protospacer adjacent motif (PAM). Cas4 enhances prespacer processing. Mechanism and structural and mechanistic model, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans ATCC BAA-125
in the presence of Cas1 and Cas2, Cas4 processes double-stranded substrates with long 3' overhangs through site-specific endonucleolytic cleavage. Cas4 recognizes PAM sequences within the prespacer and prevents integration of unprocessed prespacers, ensuring that only functional spacers will be integrated into the CRISPR array. Assays with dsDNA substrates containing blunt ends or a 24-bp duplex flanked by 15-nt 3' or 5' overhangs result in cleavage of the 3'-overhanging substrates at 65°C, but no cleavage of 5'-overhanging or blunt-end substrates by the enzyme under similar conditions. Exonucleolytic cleavage of the blunt-end substrate is observed using free Cas4, but only at very high concentrations. Sequence-specific integration and asymmetric prespacer processing by the adaptation complex
-
-
?
additional information
?
-
Halalkalibacterium halodurans C-125
Cas4 is a Cas1-Cas2-dependent endonuclease that cleaves 3' overhangs of prespacers. Cas4 cleavage is sequence and site-specific and depends on the presence of a protospacer adjacent motif (PAM). Cas4 enhances prespacer processing. Mechanism and structural and mechanistic model, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans C-125
in the presence of Cas1 and Cas2, Cas4 processes double-stranded substrates with long 3' overhangs through site-specific endonucleolytic cleavage. Cas4 recognizes PAM sequences within the prespacer and prevents integration of unprocessed prespacers, ensuring that only functional spacers will be integrated into the CRISPR array. Assays with dsDNA substrates containing blunt ends or a 24-bp duplex flanked by 15-nt 3' or 5' overhangs result in cleavage of the 3'-overhanging substrates at 65°C, but no cleavage of 5'-overhanging or blunt-end substrates by the enzyme under similar conditions. Exonucleolytic cleavage of the blunt-end substrate is observed using free Cas4, but only at very high concentrations. Sequence-specific integration and asymmetric prespacer processing by the adaptation complex
-
-
?
additional information
?
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Halalkalibacterium halodurans DSM 18197
Cas4 is a Cas1-Cas2-dependent endonuclease that cleaves 3' overhangs of prespacers. Cas4 cleavage is sequence and site-specific and depends on the presence of a protospacer adjacent motif (PAM). Cas4 enhances prespacer processing. Mechanism and structural and mechanistic model, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans DSM 18197
in the presence of Cas1 and Cas2, Cas4 processes double-stranded substrates with long 3' overhangs through site-specific endonucleolytic cleavage. Cas4 recognizes PAM sequences within the prespacer and prevents integration of unprocessed prespacers, ensuring that only functional spacers will be integrated into the CRISPR array. Assays with dsDNA substrates containing blunt ends or a 24-bp duplex flanked by 15-nt 3' or 5' overhangs result in cleavage of the 3'-overhanging substrates at 65°C, but no cleavage of 5'-overhanging or blunt-end substrates by the enzyme under similar conditions. Exonucleolytic cleavage of the blunt-end substrate is observed using free Cas4, but only at very high concentrations. Sequence-specific integration and asymmetric prespacer processing by the adaptation complex
-
-
?
additional information
?
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Halalkalibacterium halodurans FERM 7344
Cas4 is a Cas1-Cas2-dependent endonuclease that cleaves 3' overhangs of prespacers. Cas4 cleavage is sequence and site-specific and depends on the presence of a protospacer adjacent motif (PAM). Cas4 enhances prespacer processing. Mechanism and structural and mechanistic model, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans FERM 7344
in the presence of Cas1 and Cas2, Cas4 processes double-stranded substrates with long 3' overhangs through site-specific endonucleolytic cleavage. Cas4 recognizes PAM sequences within the prespacer and prevents integration of unprocessed prespacers, ensuring that only functional spacers will be integrated into the CRISPR array. Assays with dsDNA substrates containing blunt ends or a 24-bp duplex flanked by 15-nt 3' or 5' overhangs result in cleavage of the 3'-overhanging substrates at 65°C, but no cleavage of 5'-overhanging or blunt-end substrates by the enzyme under similar conditions. Exonucleolytic cleavage of the blunt-end substrate is observed using free Cas4, but only at very high concentrations. Sequence-specific integration and asymmetric prespacer processing by the adaptation complex
-
-
?
additional information
?
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Halalkalibacterium halodurans JCM 9153
Cas4 is a Cas1-Cas2-dependent endonuclease that cleaves 3' overhangs of prespacers. Cas4 cleavage is sequence and site-specific and depends on the presence of a protospacer adjacent motif (PAM). Cas4 enhances prespacer processing. Mechanism and structural and mechanistic model, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans JCM 9153
in the presence of Cas1 and Cas2, Cas4 processes double-stranded substrates with long 3' overhangs through site-specific endonucleolytic cleavage. Cas4 recognizes PAM sequences within the prespacer and prevents integration of unprocessed prespacers, ensuring that only functional spacers will be integrated into the CRISPR array. Assays with dsDNA substrates containing blunt ends or a 24-bp duplex flanked by 15-nt 3' or 5' overhangs result in cleavage of the 3'-overhanging substrates at 65°C, but no cleavage of 5'-overhanging or blunt-end substrates by the enzyme under similar conditions. Exonucleolytic cleavage of the blunt-end substrate is observed using free Cas4, but only at very high concentrations. Sequence-specific integration and asymmetric prespacer processing by the adaptation complex
-
-
?
additional information
?
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Cas4-1 trims and orients a duplexed DNA oligonucleotide pre-spacer. Nuclease activities of Cas4 proteins are essential to define PAM, length, and orientation of new spacers
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?
additional information
?
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Cas4-1 trims and orients a duplexed DNA oligonucleotide pre-spacer. Nuclease activities of Cas4 proteins are essential to define PAM, length, and orientation of new spacers
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?
additional information
?
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Cas4-1 trims and orients a duplexed DNA oligonucleotide pre-spacer. Nuclease activities of Cas4 proteins are essential to define PAM, length, and orientation of new spacers
-
-
?
additional information
?
-
Cas4 proteins contain a RecB-like nuclease domain and exhibit in vitro exonuclease activities
-
-
?
additional information
?
-
Cas4 proteins contain a RecB-like nuclease domain and exhibit in vitro exonuclease activities
-
-
?
additional information
?
-
Cas4-1 trims and orients a duplexed DNA oligonucleotide pre-spacer. Nuclease
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?
additional information
?
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Cas4-1 trims and orients a duplexed DNA oligonucleotide pre-spacer. Nuclease
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?
additional information
?
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Cas4-1 trims and orients a duplexed DNA oligonucleotide pre-spacer. Nuclease
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?
additional information
?
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Cas4-2 trims and orients a duplexed DNA oligonucleotide pre-spacer
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?
additional information
?
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Cas4-2 trims and orients a duplexed DNA oligonucleotide pre-spacer
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?
additional information
?
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Cas4-2 trims and orients a duplexed DNA oligonucleotide pre-spacer
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?
additional information
?
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the enzyme also exhibits ATP-independent DNA unwinding activity
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?
additional information
?
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the enzyme also exhibits ATP-independent DNA unwinding activity
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?
additional information
?
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the enzyme also exhibits ATP-independent DNA unwinding activity
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?
additional information
?
-
Cas4 proteins contain a RecB-like nuclease domain and exhibit in vitro exonuclease activities
-
-
?