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Conserved domains on  [gi|194328779|ref|NP_065170|]
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aspartate beta-hydroxylase domain-containing protein 2 [Homo sapiens]

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 pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 192-351 3.02e-64

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: 201.72  E-value: 3.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779  192 ERNFQTILCEFETLYKafsNCSLPQGWKMNS---TPSGEWFTFYLVNQGVCVPRNCRKCPRTYRLLGSLRTCIGNNVFGN 268
Cdd:pfam05118   1 EANWQVIRDELLALLK---QEEGLPPYEEEAlddFGDIGWKTFYLYAYGARLPENCALCPKTAALLEQPGVKASGCPRGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779  269 ACISVLSPGTVITEHYGPTNIRIRCHLGLKTPNGCELVVGGEPQCWAEGRCLLFDDSFLHAAFHEGsaeDGPRVVFMVDL 348
Cdd:pfam05118  78 AMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVPPGCRIRVGGETRTWREGECLLFDDSFEHEAWNET---DEPRVVLLVDV 154


                  ...
gi 194328779  349 WHP 351
Cdd:pfam05118 155 WRP 157
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 192-351 3.02e-64

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: 201.72  E-value: 3.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779  192 ERNFQTILCEFETLYKafsNCSLPQGWKMNS---TPSGEWFTFYLVNQGVCVPRNCRKCPRTYRLLGSLRTCIGNNVFGN 268
Cdd:pfam05118   1 EANWQVIRDELLALLK---QEEGLPPYEEEAlddFGDIGWKTFYLYAYGARLPENCALCPKTAALLEQPGVKASGCPRGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779  269 ACISVLSPGTVITEHYGPTNIRIRCHLGLKTPNGCELVVGGEPQCWAEGRCLLFDDSFLHAAFHEGsaeDGPRVVFMVDL 348
Cdd:pfam05118  78 AMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVPPGCRIRVGGETRTWREGECLLFDDSFEHEAWNET---DEPRVVLLVDV 154


                  ...
gi 194328779  349 WHP 351
Cdd:pfam05118 155 WRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 168-366 6.10e-50

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 166.98  E-value: 6.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779 168 FFLPDLPTTPYFSRdAQKHDVEVLERNFQTILCEFETLYK------AFSNCSLPQGwkmNSTPSGEWFTFYLVNQGVCVP 241
Cdd:COG3555    1 YRFSGLPTTPFFDR-AQFPWLAELEANWPTIRAELLALLAeiealpPYHDISFDQA---NIFFDRGWKRFYLYWYGERHP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779 242 RNCRKCPRTYRLLGSLRTCIgnnvfgNACISVLSPGTVITEHYGPTNIRIRCHLGLKTPN--GCELVVGGEPQCWAEGRC 319
Cdd:COG3555   77 SNCALCPKTAALLEQIPGVK------AAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNddRCRIRVDGETYSWREGEA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194328779 320 LLFDDSFLHAAFHEGsaeDGPRVVFMVDLWHPNVAAAERQALDFIFA 366
Cdd:COG3555  151 VLFDDTYEHEAWNDT---DETRVVLFCDVWRPMLSPWERAVNRLFAA 194
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 192-351 3.02e-64

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: 201.72  E-value: 3.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779  192 ERNFQTILCEFETLYKafsNCSLPQGWKMNS---TPSGEWFTFYLVNQGVCVPRNCRKCPRTYRLLGSLRTCIGNNVFGN 268
Cdd:pfam05118   1 EANWQVIRDELLALLK---QEEGLPPYEEEAlddFGDIGWKTFYLYAYGARLPENCALCPKTAALLEQPGVKASGCPRGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779  269 ACISVLSPGTVITEHYGPTNIRIRCHLGLKTPNGCELVVGGEPQCWAEGRCLLFDDSFLHAAFHEGsaeDGPRVVFMVDL 348
Cdd:pfam05118  78 AMFSRLQPGTHIPPHRGPTNGRLRCHLGLVVPPGCRIRVGGETRTWREGECLLFDDSFEHEAWNET---DEPRVVLLVDV 154


                  ...
gi 194328779  349 WHP 351
Cdd:pfam05118 155 WRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 168-366 6.10e-50

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 166.98  E-value: 6.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779 168 FFLPDLPTTPYFSRdAQKHDVEVLERNFQTILCEFETLYK------AFSNCSLPQGwkmNSTPSGEWFTFYLVNQGVCVP 241
Cdd:COG3555    1 YRFSGLPTTPFFDR-AQFPWLAELEANWPTIRAELLALLAeiealpPYHDISFDQA---NIFFDRGWKRFYLYWYGERHP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194328779 242 RNCRKCPRTYRLLGSLRTCIgnnvfgNACISVLSPGTVITEHYGPTNIRIRCHLGLKTPN--GCELVVGGEPQCWAEGRC 319
Cdd:COG3555   77 SNCALCPKTAALLEQIPGVK------AAMFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNddRCRIRVDGETYSWREGEA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194328779 320 LLFDDSFLHAAFHEGsaeDGPRVVFMVDLWHPNVAAAERQALDFIFA 366
Cdd:COG3555  151 VLFDDTYEHEAWNDT---DETRVVLFCDVWRPMLSPWERAVNRLFAA 194
 
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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