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Conserved domains on  [gi|503087195|ref|WP_013322050|]
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2OG-Fe(II) oxygenase [Gloeothece verrucosa]

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 ...
14-218 1.48e-35

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: 127.37  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  14 YRKQFEEgKPFkhVVIDNFFDPDVAQTLLQEFPLFDPQKAISETGTLGGKSVHENLGEISINYQILAEHLGSTAFLDCIS 93
Cdd:COG3751    3 LADALAA-QGY--VVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLASAAQARYLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  94 QLTGIEKLINDETF-----YGGGTHENLNGQELDPHVDFNLDERrwyHRRLNVIIFLNKEWEESWGGCLELHSnprEPDE 168
Cdd:COG3751   80 ALEELREALNSPLFlglfeYEGHFARYPPGGFYKRHLDAFRGDL---NRRLSLVLYLNPDWQPEWGGELELYD---DDGS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503087195 169 NQITALLPLFNRCVIFETNEYSwHGFtkiqLPAekqHLSRKSISIYLYTK 218
Cdd:COG3751  154 EEEVTVAPRFNRLVLFLSEEFP-HEV----LPV---GRERLSIAGWFRTR 195
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
14-218 1.48e-35

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: 127.37  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  14 YRKQFEEgKPFkhVVIDNFFDPDVAQTLLQEFPLFDPQKAISETGTLGGKSVHENLGEISINYQILAEHLGSTAFLDCIS 93
Cdd:COG3751    3 LADALAA-QGY--VVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLASAAQARYLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  94 QLTGIEKLINDETF-----YGGGTHENLNGQELDPHVDFNLDERrwyHRRLNVIIFLNKEWEESWGGCLELHSnprEPDE 168
Cdd:COG3751   80 ALEELREALNSPLFlglfeYEGHFARYPPGGFYKRHLDAFRGDL---NRRLSLVLYLNPDWQPEWGGELELYD---DDGS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503087195 169 NQITALLPLFNRCVIFETNEYSwHGFtkiqLPAekqHLSRKSISIYLYTK 218
Cdd:COG3751  154 EEEVTVAPRFNRLVLFLSEEFP-HEV----LPV---GRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
117-216 2.48e-19

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: 81.27  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  117 NGQELDPHVDFNLDERRWYHRRLNVIIFLNkEWEESWGGCLELHSNPREPDenqitaLLPLFNRCVIFETNEYSWHGFtk 196
Cdd:pfam13640   8 DGGFYKPHLDFFEGAEGGGQRRLTVVLYLN-DWEEEEGGELVLYDGDGVED------IKPKKGRLVLFPSSELSLHEV-- 78
                          90       100
                  ....*....|....*....|
gi 503087195  197 iqLPAEKQHlsRKSISIYLY 216
Cdd:pfam13640  79 --LPVTGGE--RWSITGWFR 94
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
35-193 4.83e-03

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: 36.98  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195    35 PDVAQTLLQEFPLFDPQKAISETGTLGGKSVHENlgeisINYQILAEHLGSTAFLDCISQLtgIEKLINDETFYGGGTHE 114
Cdd:smart00702   2 PAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYR-----QSNGTWLELLERDLVIERIRQR--LADFLGLLAGLPLSAED 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195   115 NL-----NGQELDPHVDFNLDERrwyhRRLNVIIFLNKeweESWGGCLELhsnPREPDENQiTALLPLFNRCVIFE-TNE 188
Cdd:smart00702  75 AQvarygPGGHYGPHVDNFLYGD----RIATFILYLND---VEEGGELVF---PGLRLMVV-ATVKPKKGDLLFFPsGHG 143

                   ....*
gi 503087195   189 YSWHG 193
Cdd:smart00702 144 RSLHG 148
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
14-218 1.48e-35

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: 127.37  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  14 YRKQFEEgKPFkhVVIDNFFDPDVAQTLLQEFPLFDPQKAISETGTLGGKSVHENLGEISINYQILAEHLGSTAFLDCIS 93
Cdd:COG3751    3 LADALAA-QGY--VVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLASAAQARYLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  94 QLTGIEKLINDETF-----YGGGTHENLNGQELDPHVDFNLDERrwyHRRLNVIIFLNKEWEESWGGCLELHSnprEPDE 168
Cdd:COG3751   80 ALEELREALNSPLFlglfeYEGHFARYPPGGFYKRHLDAFRGDL---NRRLSLVLYLNPDWQPEWGGELELYD---DDGS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503087195 169 NQITALLPLFNRCVIFETNEYSwHGFtkiqLPAekqHLSRKSISIYLYTK 218
Cdd:COG3751  154 EEEVTVAPRFNRLVLFLSEEFP-HEV----LPV---GRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
117-216 2.48e-19

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: 81.27  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195  117 NGQELDPHVDFNLDERRWYHRRLNVIIFLNkEWEESWGGCLELHSNPREPDenqitaLLPLFNRCVIFETNEYSWHGFtk 196
Cdd:pfam13640   8 DGGFYKPHLDFFEGAEGGGQRRLTVVLYLN-DWEEEEGGELVLYDGDGVED------IKPKKGRLVLFPSSELSLHEV-- 78
                          90       100
                  ....*....|....*....|
gi 503087195  197 iqLPAEKQHlsRKSISIYLY 216
Cdd:pfam13640  79 --LPVTGGE--RWSITGWFR 94
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
136-192 2.54e-08

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: 50.81  E-value: 2.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 503087195  136 HRRLNVIIFLNKEWEESWGGCLELHSNPREPDENQIT-ALLPLFNRCVIFETNE-YSWH 192
Cdd:pfam13661  21 GRRIAFILYLVENWKPDDGGALDLYDTDGHGQPADITkSIVPTWNKLVFFEVSPgHSFH 79
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
35-193 4.83e-03

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: 36.98  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195    35 PDVAQTLLQEFPLFDPQKAISETGTLGGKSVHENlgeisINYQILAEHLGSTAFLDCISQLtgIEKLINDETFYGGGTHE 114
Cdd:smart00702   2 PAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYR-----QSNGTWLELLERDLVIERIRQR--LADFLGLLAGLPLSAED 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503087195   115 NL-----NGQELDPHVDFNLDERrwyhRRLNVIIFLNKeweESWGGCLELhsnPREPDENQiTALLPLFNRCVIFE-TNE 188
Cdd:smart00702  75 AQvarygPGGHYGPHVDNFLYGD----RIATFILYLND---VEEGGELVF---PGLRLMVV-ATVKPKKGDLLFFPsGHG 143

                   ....*
gi 503087195   189 YSWHG 193
Cdd:smart00702 144 RSLHG 148
 
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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