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Conserved domains on  [gi|285397288|ref|NP_787098|]
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2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3 isoform 2 [Homo sapiens]

Protein Classification

2OG-Fe(II) oxygenase family protein( domain architecture ID 229412)

2OG-Fe(II) oxygenase family protein belongs to the large and diverse Fe(II)- and 2-oxoglutarate (2-OG)-dependent dioxygenase superfamily and may share a common reaction mechanism, using Fe(II) and the cosubstrate 2-OG in the active site to activate oxygen, resulting in the two-electron oxidation of a target substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
2OG-FeII_Oxy super family cl21496
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 162-275 3.62e-12

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


The actual alignment was detected with superfamily member smart00702:

Pssm-ID: 473886  Cd Length: 165  Bit Score: 63.56  E-value: 3.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285397288   162 YRYFGDKIQNIFSEEDFR--LYREVR------------------QKVQLTIAEAFGISASSLHLTKPTFFSRINSTEART 221
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRgeVTRGIGnpnetsqyrqsngtwlelLERDLVIERIRQRLADFLGLLAGLPLSAEDAQVARY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 285397288   222 AHDEYWHAHVDKVTYGSFDYTSLLYLSnylEDFGGGRFMFMEEGA--NKTVEPRAG 275
Cdd:smart00702  81 GPGGHYGPHVDNFLYGDRIATFILYLN---DVEEGGELVFPGLRLmvVATVKPKKG 133
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 162-275 3.62e-12

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 63.56  E-value: 3.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285397288   162 YRYFGDKIQNIFSEEDFR--LYREVR------------------QKVQLTIAEAFGISASSLHLTKPTFFSRINSTEART 221
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRgeVTRGIGnpnetsqyrqsngtwlelLERDLVIERIRQRLADFLGLLAGLPLSAEDAQVARY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 285397288   222 AHDEYWHAHVDKVTYGSFDYTSLLYLSnylEDFGGGRFMFMEEGA--NKTVEPRAG 275
Cdd:smart00702  81 GPGGHYGPHVDNFLYGDRIATFILYLN---DVEEGGELVFPGLRLmvVATVKPKKG 133
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 162-275 3.62e-12

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 63.56  E-value: 3.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285397288   162 YRYFGDKIQNIFSEEDFR--LYREVR------------------QKVQLTIAEAFGISASSLHLTKPTFFSRINSTEART 221
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRgeVTRGIGnpnetsqyrqsngtwlelLERDLVIERIRQRLADFLGLLAGLPLSAEDAQVARY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 285397288   222 AHDEYWHAHVDKVTYGSFDYTSLLYLSnylEDFGGGRFMFMEEGA--NKTVEPRAG 275
Cdd:smart00702  81 GPGGHYGPHVDNFLYGDRIATFILYLN---DVEEGGELVFPGLRLmvVATVKPKKG 133
 
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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