NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720414595|ref|XP_030110622|]
View 

2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2 isoform X1 [Mus musculus]

Protein Classification

2OG-Fe(II) oxygenase( domain architecture ID 10653727)

2OG-Fe(II) oxygenase belonging to the large and diverse Fe(II)- and 2-oxoglutarate (2-OG)-dependent dioxygenase superfamily that 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 the target substrate

CATH:  2.60.120.620
EC:  1.14.11.-
Gene Ontology:  GO:0008198|GO:0016705

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 89-223 5.02e-21

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: 86.67  E-value: 5.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414595   89 RQCQVLMYELGLDDPLvtplrERFLLPLMALLYPDYGGGYLDSHRAFVVKYALGQDLdlGCHYDNAE-----LTLNVALG 163
Cdd:smart00702  35 RQSNGTWLELLERDLV-----IERIRQRLADFLGLLAGLPLSAEDAQVARYGPGGHY--GPHVDNFLygdriATFILYLN 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720414595  164 KDFTGGALYFGGLFQAPAAlketlEVEHVVGSGILHRGGQ---LHGARPLCKGERWNLVVWLR 223
Cdd:smart00702 108 DVEEGGELVFPGLRLMVVA-----TVKPKKGDLLFFPSGHgrsLHGVCPVTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 89-223 5.02e-21

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: 86.67  E-value: 5.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414595   89 RQCQVLMYELGLDDPLvtplrERFLLPLMALLYPDYGGGYLDSHRAFVVKYALGQDLdlGCHYDNAE-----LTLNVALG 163
Cdd:smart00702  35 RQSNGTWLELLERDLV-----IERIRQRLADFLGLLAGLPLSAEDAQVARYGPGGHY--GPHVDNFLygdriATFILYLN 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720414595  164 KDFTGGALYFGGLFQAPAAlketlEVEHVVGSGILHRGGQ---LHGARPLCKGERWNLVVWLR 223
Cdd:smart00702 108 DVEEGGELVFPGLRLMVVA-----TVKPKKGDLLFFPSGHgrsLHGVCPVTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 89-223 5.02e-21

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: 86.67  E-value: 5.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414595   89 RQCQVLMYELGLDDPLvtplrERFLLPLMALLYPDYGGGYLDSHRAFVVKYALGQDLdlGCHYDNAE-----LTLNVALG 163
Cdd:smart00702  35 RQSNGTWLELLERDLV-----IERIRQRLADFLGLLAGLPLSAEDAQVARYGPGGHY--GPHVDNFLygdriATFILYLN 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720414595  164 KDFTGGALYFGGLFQAPAAlketlEVEHVVGSGILHRGGQ---LHGARPLCKGERWNLVVWLR 223
Cdd:smart00702 108 DVEEGGELVFPGLRLMVVA-----TVKPKKGDLLFFPSGHgrsLHGVCPVTRGSRWAITGWIR 165
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH