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Conserved domains on  [gi|640858813|gb|AIA47911|]
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aspartyl/asparaginyl beta-hydroxylase [Serratia sp. FS14]

Protein Classification

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

CATH:  2.60.120.10
Gene Ontology:  GO:0046872
PubMed:  14697267|19478949
SCOP:  3001825

Graphical summary

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List of domain hits

 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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813  20 RIQGQPVLDsAALFPDAERFTAQWRQIREEALTVAHDLHNIPRFHEIMSQQASISANdaRDWRMFIMKAYGQPIPHNLAR 99
Cdd:COG3555    5 GLPTTPFFD-RAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFD--RGWKRFYLYWYGERHPSNCAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813 100 CPTLAALIASSPDVLSASLSFLAPGKQVPPHRGPFRGILRGYLVLDMPKRadgaPAAVLKVDGREYRLHEGEFMLWDDTF 179
Cdd:COG3555   82 CPKTAALLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPND----DRCRIRVDGETYSWREGEAVLFDDTY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 640858813 180 EHEVWNDSPQVRTVLLLDIRRRDMPAGLRLLSGAIIALVR 219
Cdd:COG3555  158 EHEAWNDTDETRVVLFCDVWRPMLSPWERAVNRLFAAILM 197
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813  20 RIQGQPVLDsAALFPDAERFTAQWRQIREEALTVAHDLHNIPRFHEIMSQQASISANdaRDWRMFIMKAYGQPIPHNLAR 99
Cdd:COG3555    5 GLPTTPFFD-RAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFD--RGWKRFYLYWYGERHPSNCAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813 100 CPTLAALIASSPDVLSASLSFLAPGKQVPPHRGPFRGILRGYLVLDMPKRadgaPAAVLKVDGREYRLHEGEFMLWDDTF 179
Cdd:COG3555   82 CPKTAALLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPND----DRCRIRVDGETYSWREGEAVLFDDTY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 640858813 180 EHEVWNDSPQVRTVLLLDIRRRDMPAGLRLLSGAIIALVR 219
Cdd:COG3555  158 EHEAWNDTDETRVVLFCDVWRPMLSPWERAVNRLFAAILM 197
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813   40 TAQWRQIREEALTVAHDLHNIPRFHEIMSQQasisaNDARDWRMFIMKAYGQPIPHNLARCPTLAALI------ASSPDV 113
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDD-----FGDIGWKTFYLYAYGARLPENCALCPKTAALLeqpgvkASGCPR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813  114 LSASLSFLAPGKQVPPHRGPFRGILRGYLVLDMPkradgaPAAVLKVDGREYRLHEGEFMLWDDTFEHEVWNDSPQVRTV 193
Cdd:pfam05118  76 GQAMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVP------PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVV 149


                  ....*..
gi 640858813  194 LLLDIRR 200
Cdd:pfam05118 150 LLVDVWR 156
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813  20 RIQGQPVLDsAALFPDAERFTAQWRQIREEALTVAHDLHNIPRFHEIMSQQASISANdaRDWRMFIMKAYGQPIPHNLAR 99
Cdd:COG3555    5 GLPTTPFFD-RAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFD--RGWKRFYLYWYGERHPSNCAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813 100 CPTLAALIASSPDVLSASLSFLAPGKQVPPHRGPFRGILRGYLVLDMPKRadgaPAAVLKVDGREYRLHEGEFMLWDDTF 179
Cdd:COG3555   82 CPKTAALLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPND----DRCRIRVDGETYSWREGEAVLFDDTY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 640858813 180 EHEVWNDSPQVRTVLLLDIRRRDMPAGLRLLSGAIIALVR 219
Cdd:COG3555  158 EHEAWNDTDETRVVLFCDVWRPMLSPWERAVNRLFAAILM 197
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813   40 TAQWRQIREEALTVAHDLHNIPRFHEIMSQQasisaNDARDWRMFIMKAYGQPIPHNLARCPTLAALI------ASSPDV 113
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDD-----FGDIGWKTFYLYAYGARLPENCALCPKTAALLeqpgvkASGCPR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813  114 LSASLSFLAPGKQVPPHRGPFRGILRGYLVLDMPkradgaPAAVLKVDGREYRLHEGEFMLWDDTFEHEVWNDSPQVRTV 193
Cdd:pfam05118  76 GQAMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVP------PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVV 149


                  ....*..
gi 640858813  194 LLLDIRR 200
Cdd:pfam05118 150 LLVDVWR 156
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640858813  121 LAPGKQVPPHRGP----FRGILRGYLVLDmpkradgapaavlkVDGREYRLHEGEFMLWDDTFEHEVWNDSPQvrTVLLL 196
Cdd:pfam07883   5 LPPGESSPPHRHPgedeFFYVLEGEGELT--------------VDGEEVVLKAGDSVYFPAGVPHRFRNTGDE--PARLL 68


                  ..
gi 640858813  197 DI 198
Cdd:pfam07883  69 DV 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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