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Conserved domains on  [gi|94536836|ref|NP_060703|]
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prolyl 3-hydroxylase OGFOD1 isoform 1 [Homo sapiens]

Protein Classification

prolyl 3-hydroxylase family protein( domain architecture ID 10615252)

prolyl 3-hydroxylase family protein similar to prolyl 3-hydroxylase OGFOD1 (2-oxoglutarate and iron-dependent oxygenase domain containing 1) which catalyzes trans-3 prolyl hydroxylation at Pro62 of the small ribosomal subunit protein uS12 (RPS23) and is conserved from yeasts to humans

CATH:  2.60.120.620
EC:  1.14.11.7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
141-238 5.91e-54

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: 177.54  E-value: 5.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   141 MSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSP-VSFHQ 219
Cdd:pfam13661   1 MSCSRYEKGDFLLCHDDVIEGRRIAFILYLVENWKPDDGGALDLYDTDGHGQPADITKSIVPTWNKLVFFEVSPgHSFHQ 80
                          90
                  ....*....|....*....
gi 94536836   220 VSEVlSEEKSRLSISGWFH 238
Cdd:pfam13661  81 VAEV-VAEKPRLSISGWFH 98
2OG-FeII_Oxy super family cl21496
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
261-542 2.27e-33

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 pfam10637:

Pssm-ID: 473886  Cd Length: 255  Bit Score: 127.42  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   261 QDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLKPEKFTKVCEALEHGHVE---------------WSSRGPPN 325
Cdd:pfam10637   1 DDLEFLSKYINPEYLTPETVEELQETFEEESSLELEDFLNEEFADLLREYLESQDSElekelpqsskeieapWKVAGPPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   326 KRFYE---------KAEESKLPEILKECMKLFRSEALFLLLSNFTGLklhfLAPSeedemndkkeaettditeegtshsp 396
Cdd:pfam10637  81 KQRYLyldgeeardLQNEKDIESPLKELLQLFKSKAFRKWLALLTGL----VLTS------------------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   397 pepennqmaisnnsqqsneqtdpepeenetkkessvpmCQGELRHWKTGH-YTLIHDHSKAEFA-LDLILYCGC-EGWE- 472
Cdd:pfam10637 132 --------------------------------------EQILARRFRPGQdYTLATDTDGEELPrLEVTLCLTPtKGWEs 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   473 PEYGGFTSYIAKGEDEE---------------LLTVNPESNSLALVYRDRETLKFVKHINHRSleqkktfpnRTGFWDFS 537
Cdd:pfam10637 174 GEVGGYELYMAGDDDEDddaaiyrsddeddsvLLSIPPSWNSLSLVLRDEGVLKFVKYVSRNA---------KGSRWDIS 244

                  ....*
gi 94536836   538 FIYYE 542
Cdd:pfam10637 245 CEWGV 249
 
Name Accession Description Interval E-value
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
141-238 5.91e-54

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: 177.54  E-value: 5.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   141 MSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSP-VSFHQ 219
Cdd:pfam13661   1 MSCSRYEKGDFLLCHDDVIEGRRIAFILYLVENWKPDDGGALDLYDTDGHGQPADITKSIVPTWNKLVFFEVSPgHSFHQ 80
                          90
                  ....*....|....*....
gi 94536836   220 VSEVlSEEKSRLSISGWFH 238
Cdd:pfam13661  81 VAEV-VAEKPRLSISGWFH 98
Ofd1_CTDD pfam10637
Oxoglutarate and iron-dependent oxygenase degradation C-term; Ofd1 is a prolyl ...
261-542 2.27e-33

Oxoglutarate and iron-dependent oxygenase degradation C-term; Ofd1 is a prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygenase that accelerates the degradation of Sre1N in the presence of oxygen. The domain is conserved from yeasts to humans. Yeast Sre1 is the orthologue of mammalian sterol regulatory element binding protein (SREBP), and it responds to changes in oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. However, unlike the prolyl 4-hydroxylases that regulate mammalian hypoxia-inducible factor, Ofd1 uses multiple domains to regulate Sre1N degradation by oxygen; the Ofd1 N-terminal dioxygenase domain is required for oxygen sensing and this Ofd1 C-terminal domain accelerates Sre1N degradation in yeasts.


Pssm-ID: 402326  Cd Length: 255  Bit Score: 127.42  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   261 QDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLKPEKFTKVCEALEHGHVE---------------WSSRGPPN 325
Cdd:pfam10637   1 DDLEFLSKYINPEYLTPETVEELQETFEEESSLELEDFLNEEFADLLREYLESQDSElekelpqsskeieapWKVAGPPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   326 KRFYE---------KAEESKLPEILKECMKLFRSEALFLLLSNFTGLklhfLAPSeedemndkkeaettditeegtshsp 396
Cdd:pfam10637  81 KQRYLyldgeeardLQNEKDIESPLKELLQLFKSKAFRKWLALLTGL----VLTS------------------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   397 pepennqmaisnnsqqsneqtdpepeenetkkessvpmCQGELRHWKTGH-YTLIHDHSKAEFA-LDLILYCGC-EGWE- 472
Cdd:pfam10637 132 --------------------------------------EQILARRFRPGQdYTLATDTDGEELPrLEVTLCLTPtKGWEs 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   473 PEYGGFTSYIAKGEDEE---------------LLTVNPESNSLALVYRDRETLKFVKHINHRSleqkktfpnRTGFWDFS 537
Cdd:pfam10637 174 GEVGGYELYMAGDDDEDddaaiyrsddeddsvLLSIPPSWNSLSLVLRDEGVLKFVKYVSRNA---------KGSRWDIS 244

                  ....*
gi 94536836   538 FIYYE 542
Cdd:pfam10637 245 CEWGV 249
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
72-238 1.53e-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: 91.68  E-value: 1.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836     72 SQDFLEGLQKELMNLDF-HEKYNDLYKFQQSDDLKKRREPHISTL-RKILFEDFRSWLSDISKI---DLESTIDMSCAKY 146
Cdd:smart00702   1 SPAECQKLLEEAEPLGWrGEVTRGIGNPNETSQYRQSNGTWLELLeRDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836    147 EFTDALLCHDDELE--GRRIAFILYLVppwDRSMGGTLDLYSIDehfqpKQIVKSLIPSWNKLVFFEV-SPVSFHQVSEV 223
Cdd:smart00702  81 GPGGHYGPHVDNFLygDRIATFILYLN---DVEEGGELVFPGLR-----LMVVATVKPKKGDLLFFPSgHGRSLHGVCPV 152
                          170
                   ....*....|....*
gi 94536836    224 LSeeKSRLSISGWFH 238
Cdd:smart00702 153 TR--GSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
64-237 1.38e-13

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: 69.59  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836  64 CVIPNFIqSQDFLEGLQKELMNLDFHEKY----------NDLYKFQQSDDLKKRREPHISTLRKILF---EDFRSWLSDI 130
Cdd:COG3751  13 VVIDDFL-PPELAEALLAELPALDEAGAFkpagigrgldHQVNEWIRRDSILWLDEKLASAAQARYLaalEELREALNSP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836 131 SKIDLEStIDMSCAKYEFTDALLCHDDELEG---RRIAFILYLVPPWDRSMGGTLDLYSIDEhfqpKQIVKSLIPSWNKL 207
Cdd:COG3751  92 LFLGLFE-YEGHFARYPPGGFYKRHLDAFRGdlnRRLSLVLYLNPDWQPEWGGELELYDDDG----SEEEVTVAPRFNRL 166
                       170       180       190
                ....*....|....*....|....*....|
gi 94536836 208 VFFEVSPVSfHQVSEVlseEKSRLSISGWF 237
Cdd:COG3751 167 VLFLSEEFP-HEVLPV---GRERLSIAGWF 192
 
Name Accession Description Interval E-value
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
141-238 5.91e-54

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: 177.54  E-value: 5.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   141 MSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSP-VSFHQ 219
Cdd:pfam13661   1 MSCSRYEKGDFLLCHDDVIEGRRIAFILYLVENWKPDDGGALDLYDTDGHGQPADITKSIVPTWNKLVFFEVSPgHSFHQ 80
                          90
                  ....*....|....*....
gi 94536836   220 VSEVlSEEKSRLSISGWFH 238
Cdd:pfam13661  81 VAEV-VAEKPRLSISGWFH 98
Ofd1_CTDD pfam10637
Oxoglutarate and iron-dependent oxygenase degradation C-term; Ofd1 is a prolyl ...
261-542 2.27e-33

Oxoglutarate and iron-dependent oxygenase degradation C-term; Ofd1 is a prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygenase that accelerates the degradation of Sre1N in the presence of oxygen. The domain is conserved from yeasts to humans. Yeast Sre1 is the orthologue of mammalian sterol regulatory element binding protein (SREBP), and it responds to changes in oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. However, unlike the prolyl 4-hydroxylases that regulate mammalian hypoxia-inducible factor, Ofd1 uses multiple domains to regulate Sre1N degradation by oxygen; the Ofd1 N-terminal dioxygenase domain is required for oxygen sensing and this Ofd1 C-terminal domain accelerates Sre1N degradation in yeasts.


Pssm-ID: 402326  Cd Length: 255  Bit Score: 127.42  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   261 QDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLKPEKFTKVCEALEHGHVE---------------WSSRGPPN 325
Cdd:pfam10637   1 DDLEFLSKYINPEYLTPETVEELQETFEEESSLELEDFLNEEFADLLREYLESQDSElekelpqsskeieapWKVAGPPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   326 KRFYE---------KAEESKLPEILKECMKLFRSEALFLLLSNFTGLklhfLAPSeedemndkkeaettditeegtshsp 396
Cdd:pfam10637  81 KQRYLyldgeeardLQNEKDIESPLKELLQLFKSKAFRKWLALLTGL----VLTS------------------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   397 pepennqmaisnnsqqsneqtdpepeenetkkessvpmCQGELRHWKTGH-YTLIHDHSKAEFA-LDLILYCGC-EGWE- 472
Cdd:pfam10637 132 --------------------------------------EQILARRFRPGQdYTLATDTDGEELPrLEVTLCLTPtKGWEs 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   473 PEYGGFTSYIAKGEDEE---------------LLTVNPESNSLALVYRDRETLKFVKHINHRSleqkktfpnRTGFWDFS 537
Cdd:pfam10637 174 GEVGGYELYMAGDDDEDddaaiyrsddeddsvLLSIPPSWNSLSLVLRDEGVLKFVKYVSRNA---------KGSRWDIS 244

                  ....*
gi 94536836   538 FIYYE 542
Cdd:pfam10637 245 CEWGV 249
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
72-238 1.53e-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: 91.68  E-value: 1.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836     72 SQDFLEGLQKELMNLDF-HEKYNDLYKFQQSDDLKKRREPHISTL-RKILFEDFRSWLSDISKI---DLESTIDMSCAKY 146
Cdd:smart00702   1 SPAECQKLLEEAEPLGWrGEVTRGIGNPNETSQYRQSNGTWLELLeRDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836    147 EFTDALLCHDDELE--GRRIAFILYLVppwDRSMGGTLDLYSIDehfqpKQIVKSLIPSWNKLVFFEV-SPVSFHQVSEV 223
Cdd:smart00702  81 GPGGHYGPHVDNFLygDRIATFILYLN---DVEEGGELVFPGLR-----LMVVATVKPKKGDLLFFPSgHGRSLHGVCPV 152
                          170
                   ....*....|....*
gi 94536836    224 LSeeKSRLSISGWFH 238
Cdd:smart00702 153 TR--GSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
141-238 1.80e-18

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: 80.50  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836   141 MSCAKYEFTDALLCHDDELEG------RRIAFILYLvPPWDRSMGGTLDLYSIDEhfqpkqiVKSLIPSWNKLVFFEVSP 214
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGaegggqRRLTVVLYL-NDWEEEEGGELVLYDGDG-------VEDIKPKKGRLVLFPSSE 72
                          90       100
                  ....*....|....*....|....
gi 94536836   215 VSFHQVSEVLseEKSRLSISGWFH 238
Cdd:pfam13640  73 LSLHEVLPVT--GGERWSITGWFR 94
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
64-237 1.38e-13

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: 69.59  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836  64 CVIPNFIqSQDFLEGLQKELMNLDFHEKY----------NDLYKFQQSDDLKKRREPHISTLRKILF---EDFRSWLSDI 130
Cdd:COG3751  13 VVIDDFL-PPELAEALLAELPALDEAGAFkpagigrgldHQVNEWIRRDSILWLDEKLASAAQARYLaalEELREALNSP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536836 131 SKIDLEStIDMSCAKYEFTDALLCHDDELEG---RRIAFILYLVPPWDRSMGGTLDLYSIDEhfqpKQIVKSLIPSWNKL 207
Cdd:COG3751  92 LFLGLFE-YEGHFARYPPGGFYKRHLDAFRGdlnRRLSLVLYLNPDWQPEWGGELELYDDDG----SEEEVTVAPRFNRL 166
                       170       180       190
                ....*....|....*....|....*....|
gi 94536836 208 VFFEVSPVSfHQVSEVlseEKSRLSISGWF 237
Cdd:COG3751 167 VLFLSEEFP-HEVLPV---GRERLSIAGWF 192
 
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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