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aspartyl/asparaginyl beta-hydroxylase [Serratia sp. FS14]
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
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Name | Accession | Description | Interval | E-value | ||||
Asp_Arg_Hydrox super family | cl42444 | Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
20-219 | 4.56e-58 | ||||
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. The actual alignment was detected with superfamily member COG3555: Pssm-ID: 478204 Cd Length: 220 Bit Score: 183.15 E-value: 4.56e-58
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Name | Accession | Description | Interval | E-value | ||||
LpxO2 | COG3555 | Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ... |
20-219 | 4.56e-58 | ||||
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442776 Cd Length: 220 Bit Score: 183.15 E-value: 4.56e-58
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Asp_Arg_Hydrox | pfam05118 | Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
40-200 | 1.07e-48 | ||||
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: 157.04 E-value: 1.07e-48
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Name | Accession | Description | Interval | E-value | ||||
LpxO2 | COG3555 | Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ... |
20-219 | 4.56e-58 | ||||
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442776 Cd Length: 220 Bit Score: 183.15 E-value: 4.56e-58
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Asp_Arg_Hydrox | pfam05118 | Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
40-200 | 1.07e-48 | ||||
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: 157.04 E-value: 1.07e-48
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Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
121-198 | 4.01e-04 | ||||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 37.62 E-value: 4.01e-04
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Blast search parameters | ||||
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