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Conserved domains on  [gi|773014826|gb|AJY10516|]
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aspartyl/Asparaginyl beta-hydroxylase family protein [Burkholderia dolosa AU0158]

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 ...
 24-217 7.19e-54

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: 172.37  E-value: 7.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826  24 AVLDAAAFPDAGRFVRAWPAIRAEALAVARDLPRIPRFHEIMREQRDISANdaRDWRMFIMQAYGQPFARNLSRCPTVAS 103
Cdd:COG3555   10 PFFDRAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFD--RGWKRFYLYWYGERHPSNCALCPKTAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826 104 IVATSPDVLSASLSFLAPGKHIPPHRGPFRGILRGYLVLSMPKRangtPAAVLKIDGREYRLDEGHFLLWDDTFEHEVWN 183
Cdd:COG3555   88 LLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPND----DRCRIRVDGETYSWREGEAVLFDDTYEHEAWN 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 773014826 184 DSDDVRIVLLLDIRRRGMPRLLTWLSNAVIGVVR 217
Cdd:COG3555  164 DTDETRVVLFCDVWRPMLSPWERAVNRLFAAILM 197
 
Name Accession Description Interval E-value
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 24-217 7.19e-54

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 172.37  E-value: 7.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826  24 AVLDAAAFPDAGRFVRAWPAIRAEALAVARDLPRIPRFHEIMREQRDISANdaRDWRMFIMQAYGQPFARNLSRCPTVAS 103
Cdd:COG3555   10 PFFDRAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFD--RGWKRFYLYWYGERHPSNCALCPKTAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826 104 IVATSPDVLSASLSFLAPGKHIPPHRGPFRGILRGYLVLSMPKRangtPAAVLKIDGREYRLDEGHFLLWDDTFEHEVWN 183
Cdd:COG3555   88 LLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPND----DRCRIRVDGETYSWREGEAVLFDDTYEHEAWN 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 773014826 184 DSDDVRIVLLLDIRRRGMPRLLTWLSNAVIGVVR 217
Cdd:COG3555  164 DTDETRVVLFCDVWRPMLSPWERAVNRLFAAILM 197
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 39-198 7.46e-50

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: 159.74  E-value: 7.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826   39 RAWPAIRAEALAVARDLPRIPRFHEIMREQrdisaNDARDWRMFIMQAYGQPFARNLSRCPTVASIV------ATSPDVL 112
Cdd:pfam05118   2 ANWQVIRDELLALLKQEEGLPPYEEEALDD-----FGDIGWKTFYLYAYGARLPENCALCPKTAALLeqpgvkASGCPRG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826  113 SASLSFLAPGKHIPPHRGPFRGILRGYLVLSMPkrangtPAAVLKIDGREYRLDEGHFLLWDDTFEHEVWNDSDDVRIVL 192
Cdd:pfam05118  77 QAMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVP------PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVL 150


                  ....*.
gi 773014826  193 LLDIRR 198
Cdd:pfam05118 151 LVDVWR 156
 
Name Accession Description Interval E-value
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 24-217 7.19e-54

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 172.37  E-value: 7.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826  24 AVLDAAAFPDAGRFVRAWPAIRAEALAVARDLPRIPRFHEIMREQRDISANdaRDWRMFIMQAYGQPFARNLSRCPTVAS 103
Cdd:COG3555   10 PFFDRAQFPWLAELEANWPTIRAELLALLAEIEALPPYHDISFDQANIFFD--RGWKRFYLYWYGERHPSNCALCPKTAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826 104 IVATSPDVLSASLSFLAPGKHIPPHRGPFRGILRGYLVLSMPKRangtPAAVLKIDGREYRLDEGHFLLWDDTFEHEVWN 183
Cdd:COG3555   88 LLEQIPGVKAAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPND----DRCRIRVDGETYSWREGEAVLFDDTYEHEAWN 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 773014826 184 DSDDVRIVLLLDIRRRGMPRLLTWLSNAVIGVVR 217
Cdd:COG3555  164 DTDETRVVLFCDVWRPMLSPWERAVNRLFAAILM 197
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 39-198 7.46e-50

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: 159.74  E-value: 7.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826   39 RAWPAIRAEALAVARDLPRIPRFHEIMREQrdisaNDARDWRMFIMQAYGQPFARNLSRCPTVASIV------ATSPDVL 112
Cdd:pfam05118   2 ANWQVIRDELLALLKQEEGLPPYEEEALDD-----FGDIGWKTFYLYAYGARLPENCALCPKTAALLeqpgvkASGCPRG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826  113 SASLSFLAPGKHIPPHRGPFRGILRGYLVLSMPkrangtPAAVLKIDGREYRLDEGHFLLWDDTFEHEVWNDSDDVRIVL 192
Cdd:pfam05118  77 QAMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVP------PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVL 150


                  ....*.
gi 773014826  193 LLDIRR 198
Cdd:pfam05118 151 LVDVWR 156
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
92-194 2.75e-03

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 35.98  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773014826  92 ARNLSRCPTVASIVATSPDVLSASLSFLAPGKHIPPHRGPFRGILrgyLVLSmpkranGTpaAVLKIDGREYRLDEGHFL 171
Cdd:COG1917    3 LAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELI---YVLE------GE--GEVEVGGEEYELKPGDVV 71

                         90       100
                 ....*....|....*....|...
gi 773014826 172 LWDDTFEHEVWNDSDDVRIVLLL 194
Cdd:COG1917   72 FIPPGVPHAFRNLGDEPAVLLVV 94
 
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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