RecName: Full=Aspartate beta-hydroxylase domain-containing protein 2
aspartyl/asparaginyl beta-hydroxylase domain-containing protein( domain architecture ID 10523946)
aspartyl/asparaginyl beta-hydroxylase domain-containing protein is an iron (II)/2-oxoglutarate-dependent oxygenase which catalyzes an oxidative reaction in one of a wide range of metabolic processes; belongs to the cupin superfamily
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Asp_Arg_Hydrox | pfam05118 | Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
166-325 | 2.87e-62 | |||
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins. : Pssm-ID: 461552 Cd Length: 157 Bit Score: 195.56 E-value: 2.87e-62
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Name | Accession | Description | Interval | E-value | ||||
Asp_Arg_Hydrox | pfam05118 | Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
166-325 | 2.87e-62 | ||||
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins. Pssm-ID: 461552 Cd Length: 157 Bit Score: 195.56 E-value: 2.87e-62
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LpxO2 | COG3555 | Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ... |
142-340 | 4.34e-48 | ||||
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442776 Cd Length: 220 Bit Score: 161.20 E-value: 4.34e-48
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Name | Accession | Description | Interval | E-value | ||||
Asp_Arg_Hydrox | pfam05118 | Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
166-325 | 2.87e-62 | ||||
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins. Pssm-ID: 461552 Cd Length: 157 Bit Score: 195.56 E-value: 2.87e-62
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LpxO2 | COG3555 | Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ... |
142-340 | 4.34e-48 | ||||
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442776 Cd Length: 220 Bit Score: 161.20 E-value: 4.34e-48
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Blast search parameters | ||||
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