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polynucleotide kinase [Gordonia phage MelBins]
HAD family hydrolase( domain architecture ID 229399)
HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
HAD_like super family | cl21460 | Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ... |
20-159 | 8.68e-13 | |||
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions. The actual alignment was detected with superfamily member cd07502: Pssm-ID: 473868 Cd Length: 145 Bit Score: 62.55 E-value: 8.68e-13
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Name | Accession | Description | Interval | E-value | ||||
HAD_PNKP-C | cd07502 | C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ... |
20-159 | 8.68e-13 | ||||
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319805 Cd Length: 145 Bit Score: 62.55 E-value: 8.68e-13
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pseT | PHA02530 | polynucleotide kinase; Provisional |
20-159 | 9.45e-09 | ||||
polynucleotide kinase; Provisional Pssm-ID: 222856 [Multi-domain] Cd Length: 300 Bit Score: 53.49 E-value: 9.45e-09
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YqfW | COG5663 | Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; |
25-165 | 6.06e-08 | ||||
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; Pssm-ID: 444382 [Multi-domain] Cd Length: 187 Bit Score: 50.23 E-value: 6.06e-08
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Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
22-162 | 6.30e-03 | ||||
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria. Pssm-ID: 459910 [Multi-domain] Cd Length: 191 Bit Score: 36.02 E-value: 6.30e-03
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Name | Accession | Description | Interval | E-value | ||||
HAD_PNKP-C | cd07502 | C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ... |
20-159 | 8.68e-13 | ||||
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319805 Cd Length: 145 Bit Score: 62.55 E-value: 8.68e-13
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pseT | PHA02530 | polynucleotide kinase; Provisional |
20-159 | 9.45e-09 | ||||
polynucleotide kinase; Provisional Pssm-ID: 222856 [Multi-domain] Cd Length: 300 Bit Score: 53.49 E-value: 9.45e-09
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YqfW | COG5663 | Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; |
25-165 | 6.06e-08 | ||||
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; Pssm-ID: 444382 [Multi-domain] Cd Length: 187 Bit Score: 50.23 E-value: 6.06e-08
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HAD_BPGM-like | cd07505 | beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ... |
22-111 | 8.75e-04 | ||||
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319808 [Multi-domain] Cd Length: 143 Bit Score: 37.98 E-value: 8.75e-04
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Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
22-162 | 6.30e-03 | ||||
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria. Pssm-ID: 459910 [Multi-domain] Cd Length: 191 Bit Score: 36.02 E-value: 6.30e-03
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Blast search parameters | ||||
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