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Conserved domains on  [gi|576865062|pdb|4IW3|A]
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Chain A, Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) in complex with elongation factor Tu (EF-Tu)

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 ...
33-224 3.22e-77

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: 230.99  E-value: 3.22e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A       33 AAVVDDLATHGWSQQAHFLPADLVRALAAECRRRDAEGELNPAGVGRGATQEVRETIRGDQIQWIDPGQA-EACDQYLAA 111
Cdd:COG3751   1 AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLAsAAQARYLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A      112 MDQLRLAINQGLFLGLEDFECHFALYPPGAFYRRHLDRFRDDDRRMVSAVLYLNEGWQPHDGGQLRMFLADG--VEHDVE 189
Cdd:COG3751  81 LEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPEWGGELELYDDDGseEEVTVA 160
                       170       180       190
                ....*....|....*....|....*....|....*
4IW3_A      190 PVAGCLVVFLSGEVPHEVLPAGRERLSLTGWFRRR 224
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 ...
33-224 3.22e-77

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: 230.99  E-value: 3.22e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A       33 AAVVDDLATHGWSQQAHFLPADLVRALAAECRRRDAEGELNPAGVGRGATQEVRETIRGDQIQWIDPGQA-EACDQYLAA 111
Cdd:COG3751   1 AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLAsAAQARYLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A      112 MDQLRLAINQGLFLGLEDFECHFALYPPGAFYRRHLDRFRDDDRRMVSAVLYLNEGWQPHDGGQLRMFLADG--VEHDVE 189
Cdd:COG3751  81 LEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPEWGGELELYDDDGseEEVTVA 160
                       170       180       190
                ....*....|....*....|....*....|....*
4IW3_A      190 PVAGCLVVFLSGEVPHEVLPAGRERLSLTGWFRRR 224
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 ...
132-222 2.67e-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: 79.34  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A        132 CHFALYPPGAFYRR---HLDRFRDDDRRMVSAVLYLNEgWQPHDGGQLRMFLADGVEhDVEPVAGCLVVFLSGEV-PHEV 207
Cdd:pfam13640   1 LQLARYGDGGFYKPhldFFEGAEGGGQRRLTVVLYLND-WEEEEGGELVLYDGDGVE-DIKPKKGRLVLFPSSELsLHEV 78
                          90
                  ....*....|....*.
4IW3_A        208 LPA-GRERLSLTGWFR 222
Cdd:pfam13640  79 LPVtGGERWSITGWFR 94
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
68-222 5.70e-19

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: 80.51  E-value: 5.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A          68 AEGELNPAGVGRGAT-QEVRETIRGDQIQWIDPGQAEACDQYLaaMDQLRLAINQGLFLGLEDFECHFALYPPGAFYrRH 146
Cdd:smart00702  12 AEPLGWRGEVTRGIGnPNETSQYRQSNGTWLELLERDLVIERI--RQRLADFLGLLAGLPLSAEDAQVARYGPGGHY-GP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A         147 LDRFRDDDRRMVSAVLYLNEgwqPHDGGQLRMFLADG-VEHDVEPVAGCLVVFLSGEV--PHEVLPAGR-ERLSLTGWFR 222
Cdd:smart00702  89 HVDNFLYGDRIATFILYLND---VEEGGELVFPGLRLmVVATVKPKKGDLLFFPSGHGrsLHGVCPVTRgSRWAITGWIR 165
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
33-224 3.22e-77

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: 230.99  E-value: 3.22e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A       33 AAVVDDLATHGWSQQAHFLPADLVRALAAECRRRDAEGELNPAGVGRGATQEVRETIRGDQIQWIDPGQA-EACDQYLAA 111
Cdd:COG3751   1 AALADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQVNEWIRRDSILWLDEKLAsAAQARYLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A      112 MDQLRLAINQGLFLGLEDFECHFALYPPGAFYRRHLDRFRDDDRRMVSAVLYLNEGWQPHDGGQLRMFLADG--VEHDVE 189
Cdd:COG3751  81 LEELREALNSPLFLGLFEYEGHFARYPPGGFYKRHLDAFRGDLNRRLSLVLYLNPDWQPEWGGELELYDDDGseEEVTVA 160
                       170       180       190
                ....*....|....*....|....*....|....*
4IW3_A      190 PVAGCLVVFLSGEVPHEVLPAGRERLSLTGWFRRR 224
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 ...
132-222 2.67e-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: 79.34  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A        132 CHFALYPPGAFYRR---HLDRFRDDDRRMVSAVLYLNEgWQPHDGGQLRMFLADGVEhDVEPVAGCLVVFLSGEV-PHEV 207
Cdd:pfam13640   1 LQLARYGDGGFYKPhldFFEGAEGGGQRRLTVVLYLND-WEEEEGGELVLYDGDGVE-DIKPKKGRLVLFPSSELsLHEV 78
                          90
                  ....*....|....*.
4IW3_A        208 LPA-GRERLSLTGWFR 222
Cdd:pfam13640  79 LPVtGGERWSITGWFR 94
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
68-222 5.70e-19

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: 80.51  E-value: 5.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A          68 AEGELNPAGVGRGAT-QEVRETIRGDQIQWIDPGQAEACDQYLaaMDQLRLAINQGLFLGLEDFECHFALYPPGAFYrRH 146
Cdd:smart00702  12 AEPLGWRGEVTRGIGnPNETSQYRQSNGTWLELLERDLVIERI--RQRLADFLGLLAGLPLSAEDAQVARYGPGGHY-GP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IW3_A         147 LDRFRDDDRRMVSAVLYLNEgwqPHDGGQLRMFLADG-VEHDVEPVAGCLVVFLSGEV--PHEVLPAGR-ERLSLTGWFR 222
Cdd:smart00702  89 HVDNFLYGDRIATFILYLND---VEEGGELVFPGLRLmVVATVKPKKGDLLFFPSGHGrsLHGVCPVTRgSRWAITGWIR 165
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
158-222 8.68e-13

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: 62.36  E-value: 8.68e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4IW3_A        158 VSAVLYLNEGWQPHDGGQLRMFLADG------VEHDVEPVAGCLVVFLS--GEVPHEVLP--AGRERLSLTGWFR 222
Cdd:pfam13661  24 IAFILYLVENWKPDDGGALDLYDTDGhgqpadITKSIVPTWNKLVFFEVspGHSFHQVAEvvAEKPRLSISGWFH 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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