deoxyribonuclease-2-beta isoform X1 [Mus musculus]
Protein Classification
deoxyribonuclease II family protein( domain architecture ID 12043216)
deoxyribonuclease II family protein similar to human deoxyribonuclease-2-alpha and deoxyribonuclease-2-beta which hydrolyze DNA
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| DNase_II | pfam03265 | Deoxyribonuclease II; |
27-342 | 6.03e-159 | |||||
Deoxyribonuclease II; : Pssm-ID: 460868 [Multi-domain] Cd Length: 316 Bit Score: 447.87 E-value: 6.03e-159
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| Name | Accession | Description | Interval | E-value | |||||
| DNase_II | pfam03265 | Deoxyribonuclease II; |
27-342 | 6.03e-159 | |||||
Deoxyribonuclease II; Pssm-ID: 460868 [Multi-domain] Cd Length: 316 Bit Score: 447.87 E-value: 6.03e-159
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| PLDc_DNaseII_beta_2 | cd09192 | Catalytic domain, repeat 2, of Deoxyribonuclease II beta and similar proteins; Catalytic ... |
214-353 | 3.56e-93 | |||||
Catalytic domain, repeat 2, of Deoxyribonuclease II beta and similar proteins; Catalytic domain, repeat 2, of Deoxyribonuclease II beta (DNase II beta, EC 3.1.22.1), also known as DNase II-like acid DNase (DLAD), and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II beta, or DLAD, is a novel mammalian divalent cation-independent endonuclease with homology to DNase II alpha. It is highly expressed in the eye lens and in salivary glands and is responsible for the degradation of nuclear DNA during lens cell differentiation. DLAD mainly exists as a cytoplasmic protein and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. Like DNase II alpha, DLAD is active under acidic conditions with maximum activity at pH 5.2. Aurintricarboxylic acid and Zn2+ are effective inhibitors of DLAD activity. Mice deficient in DLAD develop cataracts as they are unable to degrade DNA during differentiation of the lens cells. Pssm-ID: 197288 Cd Length: 139 Bit Score: 274.36 E-value: 3.56e-93
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| Name | Accession | Description | Interval | E-value | |||||
| DNase_II | pfam03265 | Deoxyribonuclease II; |
27-342 | 6.03e-159 | |||||
Deoxyribonuclease II; Pssm-ID: 460868 [Multi-domain] Cd Length: 316 Bit Score: 447.87 E-value: 6.03e-159
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| PLDc_DNaseII_beta_2 | cd09192 | Catalytic domain, repeat 2, of Deoxyribonuclease II beta and similar proteins; Catalytic ... |
214-353 | 3.56e-93 | |||||
Catalytic domain, repeat 2, of Deoxyribonuclease II beta and similar proteins; Catalytic domain, repeat 2, of Deoxyribonuclease II beta (DNase II beta, EC 3.1.22.1), also known as DNase II-like acid DNase (DLAD), and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II beta, or DLAD, is a novel mammalian divalent cation-independent endonuclease with homology to DNase II alpha. It is highly expressed in the eye lens and in salivary glands and is responsible for the degradation of nuclear DNA during lens cell differentiation. DLAD mainly exists as a cytoplasmic protein and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. Like DNase II alpha, DLAD is active under acidic conditions with maximum activity at pH 5.2. Aurintricarboxylic acid and Zn2+ are effective inhibitors of DLAD activity. Mice deficient in DLAD develop cataracts as they are unable to degrade DNA during differentiation of the lens cells. Pssm-ID: 197288 Cd Length: 139 Bit Score: 274.36 E-value: 3.56e-93
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| PLDc_DNaseII_beta_1 | cd09190 | Catalytic domain, repeat 1, of Deoxyribonuclease II beta and similar proteins; Catalytic ... |
25-184 | 1.28e-82 | |||||
Catalytic domain, repeat 1, of Deoxyribonuclease II beta and similar proteins; Catalytic domain, repeat 1, of Deoxyribonuclease II beta (DNase II beta, EC 3.1.22.1), also known as DNase II-like acid DNase (DLAD), and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II beta, or DLAD, is a novel mammalian divalent cation-independent endonuclease with homology to DNase II alpha. It is highly expressed in the eye lens and in salivary glands and is responsible for the degradation of nuclear DNA during lens cell differentiation. DLAD mainly exists as a cytoplasmic protein and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. Like DNase II alpha, DLAD is active under acidic conditions with maximum activity at pH 5.2. Aurintricarboxylic acid and Zn2+ are effective inhibitors of DLAD activity. Mice deficient in DLAD develop cataracts as they are unable to degrade DNA during differentiation of the lens cells. Pssm-ID: 197286 Cd Length: 165 Bit Score: 248.24 E-value: 1.28e-82
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| PLDc_DNaseII_2 | cd09121 | Catalytic domain, repeat 2, of Deoxyribonuclease II and similar proteins; Catalytic domain, ... |
215-353 | 1.39e-61 | |||||
Catalytic domain, repeat 2, of Deoxyribonuclease II and similar proteins; Catalytic domain, repeat 2, of Deoxyribonuclease II (DNase II, EC 3.1.22.1), an endodeoxyribonuclease with ubiquitous tissue distribution. It is essential for accessory apoptotic DNA fragmentation and DNA clearance during development, as well as in tissue regeneration in higher eukaryotes. Unlike the majority of nucleases, DNase II functions optimally at acidic pH in the absence of divalent metal ion cofactors. It hydrolyzes the phosphodiester backbone of DNA by a single strand cleavage mechanism to generate 3'-phosphate termini. The majority of family members contain an N-terminal signal-peptide leader sequence, which is critical for N-glycosylation and DNase II activity. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta (also known as DNase II-like acid DNase, DLAD) subtypes. A few homologs are found in non-metazoan species, but none are found in fungi, plants or prokaryotes, with the sole exception of Burkholderia pseudomallei. Among those homologs, the Caenorhabditis elegans C07B5.5 ORF encoding NUC-1 apoptotic nuclease, the uncharacterized C. elegans crn-6 (cell death related nuclease) gene encoding protein, and the putative gene CG7780 encoding Drosophila DNase II (dDNase II) have similar cleavage activity and specificity to mammalian DNase II enzymes. They may function like an acid DNase implicated in degrading DNA from apoptotic cells engulfed by macrophages. Plancitoxin I, the major lethal factor from the Acanthaster planci venom, is a unique homolog of mammalian DNase II. It has potent hepatotoxicity and the optimum pH for its activity is 7.2, unlike the optimum acidic PH for mammalian DNase II. Some members of this family contain substitutions of conserved residues found in the putative active site, which suggest that these proteins may have diverged from the canonical DNase II activity and may perform other functions. Pssm-ID: 197220 Cd Length: 139 Bit Score: 193.60 E-value: 1.39e-61
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| PLDc_DNaseII_1 | cd09120 | Catalytic domain, repeat 1, of Deoxyribonuclease II and similar proteins; Catalytic domain, ... |
25-167 | 2.01e-56 | |||||
Catalytic domain, repeat 1, of Deoxyribonuclease II and similar proteins; Catalytic domain, repeat 1, of Deoxyribonuclease II (DNase II, EC 3.1.22.1), an endodeoxyribonuclease with ubiquitous tissue distribution. It is essential for accessory apoptotic DNA fragmentation and DNA clearance during development, as well as in tissue regeneration in higher eukaryotes. Unlike the majority of nucleases, DNase II functions optimally at acidic pH in the absence of divalent metal ion cofactors. It hydrolyzes the phosphodiester backbone of DNA by a single strand cleavage mechanism to generate 3'-phosphate termini. The majority of family members contain an N-terminal signal-peptide leader sequence, which is critical for N-glycosylation and DNase II activity. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta (also known as DNase II-like acid DNase, DLAD) subtypes. A few homologs are found in non-metazoan species, but none are found in fungi, plants or prokaryotes, with the sole exception of Burkholderia pseudomallei. Among those homologs, the Caenorhabditis elegans C07B5.5 ORF encoding NUC-1 apoptotic nuclease, the uncharacterized C. elegans crn-6 (cell death related nuclease) gene encoding protein, and the putative gene CG7780 encoding Drosophila DNase II (dDNase II) have similar cleavage activity and specificity to mammalian DNase II enzymes. They may function like an acid DNase implicated in degrading DNA from apoptotic cells engulfed by macrophages. Plancitoxin I, the major lethal factor from the Acanthaster planci venom, is a unique homolog of mammalian DNase II. It has potent hepatotoxicity and the optimum pH for its activity is 7.2, unlike the optimum acidic PH for mammalian DNase II. Some members of this family contain substitutions of conserved residues found in the putative active site, which suggest that these proteins may have diverged from a canonical DNase II activity and may perform other functions. Pssm-ID: 197219 Cd Length: 141 Bit Score: 180.57 E-value: 2.01e-56
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| PLDc_DNaseII_alpha_1 | cd09189 | Catalytic domain, repeat 1, of Deoxyribonuclease II alpha and similar proteins; Catalytic ... |
26-181 | 8.05e-48 | |||||
Catalytic domain, repeat 1, of Deoxyribonuclease II alpha and similar proteins; Catalytic domain, repeat 1, of Deoxyribonuclease II alpha (DNase II alpha, EC 3.1.22.1) and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II alpha is an acidic endonuclease found in lysosomes, nuclei, and various secretions. It plays a critical role in the degradation of nuclear DNA expelled from erythroid precursor cells, as well as in the degradation of the apoptotic DNA after macrophages engulf them. It cleaves double-stranded DNA to short 3'-phosphoryl oligonucleotides, rather than 3'-hydroxyl groups, and functions optimally at acidic pH in the absence of divalent metal ion cofactors. Pssm-ID: 197285 Cd Length: 162 Bit Score: 158.93 E-value: 8.05e-48
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| PLDc_DNaseII_alpha_2 | cd09191 | Catalytic domain, repeat 2, of Deoxyribonuclease II alpha and similar proteins; Catalytic ... |
222-353 | 5.17e-41 | |||||
Catalytic domain, repeat 2, of Deoxyribonuclease II alpha and similar proteins; Catalytic domain, repeat 2, of Deoxyribonuclease II alpha (DNase II alpha, EC 3.1.22.1) and similar proteins. DNase II is a monomeric nuclease that contains two copies of a variant HKD motif, where the aspartic acid residue is not conserved. The HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. The catalytic center of DNase II is formed by the two variant HKD motifs from the N- and C-terminal domains in a pseudodimeric way. Members of this family are mainly found in metazoans, and vertebrate proteins have been further classified into DNase II alpha and beta. DNase II alpha is an acidic endonuclease found in lysosomes, nuclei, and various secretions. It plays a critical role in the degradation of nuclear DNA expelled from erythroid precursor cells, as well as in the degradation of the apoptotic DNA after macrophages engulf them. It cleaves double-stranded DNA to short 3'-phosphoryl oligonucleotides, rather than 3'-hydroxyl groups, and functions optimally at acidic pH in the absence of divalent metal ion cofactors. Pssm-ID: 197287 Cd Length: 137 Bit Score: 140.45 E-value: 5.17e-41
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