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Conserved domains on  [gi|504408256|ref|WP_014595358|]
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MULTISPECIES: 2OG-Fe(II) oxygenase [Stutzerimonas]

Protein Classification

2OG-Fe(II) oxygenase( domain architecture ID 10790396)

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; such as prolyl 4-hydroxylase subunit alpha, part of the heterotetrameric enzyme that catalyzes the post-translational formation of 4-hydroxyproline

CATH:  2.60.120.620
EC:  1.14.11.-
Gene Ontology:  GO:0008198|GO:0016705
PubMed:  27561929|11276424

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
4-195 5.93e-85

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 249.48  E-value: 5.93e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256   4 SSIIDDLAERGWSLQSSFLPSDVTHKLADECRKREAEGALAPAGVGRGEAQAVREGIRSDHIQWLEPG-QSPVCDDYLEV 82
Cdd:COG3751    1 AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKlASAAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256  83 MDGLRQQLNRELFLGLEEFECHFAFYPPGAFYQTHLDRFRDDDSRSVTAVLYLNPDWQPAHAGELRMHMPDGS--QLDVP 160
Cdd:COG3751   81 LEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPEWGGELELYDDDGSeeEVTVA 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504408256 161 PLAGNLVVFLSGEFPHEVLVTQADRLSLTGWFRRR 195
Cdd:COG3751  161 PRFNRLVLFLSEEFPHEVLPVGRERLSIAGWFRTR 195
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
4-195 5.93e-85

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 249.48  E-value: 5.93e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256   4 SSIIDDLAERGWSLQSSFLPSDVTHKLADECRKREAEGALAPAGVGRGEAQAVREGIRSDHIQWLEPG-QSPVCDDYLEV 82
Cdd:COG3751    1 AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKlASAAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256  83 MDGLRQQLNRELFLGLEEFECHFAFYPPGAFYQTHLDRFRDDDSRSVTAVLYLNPDWQPAHAGELRMHMPDGS--QLDVP 160
Cdd:COG3751   81 LEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPEWGGELELYDDDGSeeEVTVA 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504408256 161 PLAGNLVVFLSGEFPHEVLVTQADRLSLTGWFRRR 195
Cdd:COG3751  161 PRFNRLVLFLSEEFPHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
103-193 6.76e-24

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 90.51  E-value: 6.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256  103 CHFAFYPPGAFYQTHLDRFRDDDS---RSVTAVLYLNpDWQPAHAGELRMHMPDGSQlDVPPLAGNLVVFLSGE-FPHEV 178
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGggqRRLTVVLYLN-DWEEEEGGELVLYDGDGVE-DIKPKKGRLVLFPSSElSLHEV 78
                          90
                  ....*....|....*.
gi 504408256  179 L-VTQADRLSLTGWFR 193
Cdd:pfam13640  79 LpVTGGERWSITGWFR 94
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
31-193 1.09e-23

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: 92.07  E-value: 1.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256    31 ADECRK--REAEGALAPAGVGRGEA-QAVREGIRSDHIQWLEPgqspvcDDYLEVMDGLRQQL----NRELFLGLEEFEC 103
Cdd:smart00702   2 PAECQKllEEAEPLGWRGEVTRGIGnPNETSQYRQSNGTWLEL------LERDLVIERIRQRLadflGLLAGLPLSAEDA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256   104 HFAFYPPGAFYQTHLDRFRDDDsRSVTAVLYLNpdwQPAHAGELRMH-MPDGSQLDVPPLAGNLVVFLSG--EFPHEVL- 179
Cdd:smart00702  76 QVARYGPGGHYGPHVDNFLYGD-RIATFILYLN---DVEEGGELVFPgLRLMVVATVKPKKGDLLFFPSGhgRSLHGVCp 151
                          170
                   ....*....|....
gi 504408256   180 VTQADRLSLTGWFR 193
Cdd:smart00702 152 VTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
4-195 5.93e-85

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 249.48  E-value: 5.93e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256   4 SSIIDDLAERGWSLQSSFLPSDVTHKLADECRKREAEGALAPAGVGRGEAQAVREGIRSDHIQWLEPG-QSPVCDDYLEV 82
Cdd:COG3751    1 AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKlASAAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256  83 MDGLRQQLNRELFLGLEEFECHFAFYPPGAFYQTHLDRFRDDDSRSVTAVLYLNPDWQPAHAGELRMHMPDGS--QLDVP 160
Cdd:COG3751   81 LEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPEWGGELELYDDDGSeeEVTVA 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504408256 161 PLAGNLVVFLSGEFPHEVLVTQADRLSLTGWFRRR 195
Cdd:COG3751  161 PRFNRLVLFLSEEFPHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
103-193 6.76e-24

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 90.51  E-value: 6.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256  103 CHFAFYPPGAFYQTHLDRFRDDDS---RSVTAVLYLNpDWQPAHAGELRMHMPDGSQlDVPPLAGNLVVFLSGE-FPHEV 178
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGggqRRLTVVLYLN-DWEEEEGGELVLYDGDGVE-DIKPKKGRLVLFPSSElSLHEV 78
                          90
                  ....*....|....*.
gi 504408256  179 L-VTQADRLSLTGWFR 193
Cdd:pfam13640  79 LpVTGGERWSITGWFR 94
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
31-193 1.09e-23

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: 92.07  E-value: 1.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256    31 ADECRK--REAEGALAPAGVGRGEA-QAVREGIRSDHIQWLEPgqspvcDDYLEVMDGLRQQL----NRELFLGLEEFEC 103
Cdd:smart00702   2 PAECQKllEEAEPLGWRGEVTRGIGnPNETSQYRQSNGTWLEL------LERDLVIERIRQRLadflGLLAGLPLSAEDA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256   104 HFAFYPPGAFYQTHLDRFRDDDsRSVTAVLYLNpdwQPAHAGELRMH-MPDGSQLDVPPLAGNLVVFLSG--EFPHEVL- 179
Cdd:smart00702  76 QVARYGPGGHYGPHVDNFLYGD-RIATFILYLN---DVEEGGELVFPgLRLMVVATVKPKKGDLLFFPSGhgRSLHGVCp 151
                          170
                   ....*....|....
gi 504408256   180 VTQADRLSLTGWFR 193
Cdd:smart00702 152 VTRGSRWAITGWIR 165
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
104-193 9.21e-16

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 433386  Cd Length: 98  Bit Score: 69.68  E-value: 9.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408256  104 HFAFYPPGAFYQTHLDRFRDddsRSVTAVLYLNPDWQPAHAGELRMHMPDGSQL------DVPPLAGNLVVFLS--GEFP 175
Cdd:pfam13661   2 SCSRYEKGDFLLCHDDVIEG---RRIAFILYLVENWKPDDGGALDLYDTDGHGQpaditkSIVPTWNKLVFFEVspGHSF 78
                          90       100
                  ....*....|....*....|
gi 504408256  176 HEVL--VTQADRLSLTGWFR 193
Cdd:pfam13661  79 HQVAevVAEKPRLSISGWFH 98
 
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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