5'-deoxynucleotidase HDDC2 isoform X3 [Mus musculus]
Protein Classification
HD domain-containing protein( domain architecture ID 229447)
HD domain-containing protein may function as a metal dependent phosphohydrolase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| HDc super family | cl21469 | Metal dependent phosphohydrolases with conserved 'HD' motif |
110-177 | 1.93e-27 | ||
Metal dependent phosphohydrolases with conserved 'HD' motif The actual alignment was detected with superfamily member pfam13023: Pssm-ID: 473873 Cd Length: 163 Bit Score: 101.52 E-value: 1.93e-27
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| Name | Accession | Description | Interval | E-value | ||
| HD_3 | pfam13023 | HD domain; HD domains are metal dependent phosphohydrolases. |
110-177 | 1.93e-27 | ||
HD domain; HD domains are metal dependent phosphohydrolases. Pssm-ID: 432939 Cd Length: 163 Bit Score: 101.52 E-value: 1.93e-27
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| YfbR | COG1896 | 5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ... |
110-170 | 3.33e-14 | ||
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only]; Pssm-ID: 441500 Cd Length: 162 Bit Score: 67.20 E-value: 3.33e-14
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| Name | Accession | Description | Interval | E-value | ||
| HD_3 | pfam13023 | HD domain; HD domains are metal dependent phosphohydrolases. |
110-177 | 1.93e-27 | ||
HD domain; HD domains are metal dependent phosphohydrolases. Pssm-ID: 432939 Cd Length: 163 Bit Score: 101.52 E-value: 1.93e-27
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| YfbR | COG1896 | 5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ... |
110-170 | 3.33e-14 | ||
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only]; Pssm-ID: 441500 Cd Length: 162 Bit Score: 67.20 E-value: 3.33e-14
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| YfbR-like | pfam12917 | 5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5 ... |
121-170 | 1.32e-03 | ||
5'-deoxynucleotidase YfbR-like; This entry contains Escherichia coli (strain K12) YfbR. It a 5'-deoxynucleotidase that functions as a dCMP phosphohydrolase in a salvage pathway for the synthesis of dUMP in a dcd/deoA mutant. YfbR contains a conserved HD domain. YfbR has phosphatase activity with deoxyribonucleoside 5'-monophosphates and does not hydrolyze ribonucleotides or deoxyribonucloside 3'-monophosphates. Crystal structures of YfbR have been solved, it was suggested that the biological unit is a dimer. This family also includes phage HD domain-containing hydrolase-like enzymes, such as A0A2H5BHG9 and A0A2L0V156 from Acinetobacter phage SH-Ab15497, which are associated with PurZ, an enzyme that catalyzes the synthesis of diaminopurine (Z), a DNA modification that gives phages an advantage for evading host restriction enzymes activity. They have 2'-deoxyadenine 5'-triphosphate triphosphohydrolase (dATPase) activity and catalyze the hydrolysis of 2'-deoxyadenine 5'-triphosphate dATP to 2'-deoxyadenine (dA) and triphosphate. These enzymes are highly specific for dATP and also catalyze the hydrolysis of dADP and dAMP into dA, releasing pyrophosphate and phosphate, respectively. Thus, these dATPases facilitate the synthesis of Z-genome synthesis removing dATP and dADP from the nucleotide pool of the host. Pssm-ID: 432874 Cd Length: 182 Bit Score: 37.87 E-value: 1.32e-03
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