NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|809281406|ref|NP_001295032|]
View 

prolyl hydroxylase EGLN3 isoform 2 [Homo sapiens]

Protein Classification

prolyl hydroxylase family protein( domain architecture ID 10653727)

prolyl hydroxylase family protein similar to prolyl 3-hydroxylase 1, a member of the 2-oxoglutarate dioxygenase superfamily, plays a crucial role in collagen synthesis, folding, and assembly

CATH:  2.60.120.620
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 ...
 24-119 2.69e-31

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: 109.78  E-value: 2.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406    24 HEAMVACYPGnGTGYVRHVDNPNGDGRCITCIYYLNKnwdaKLHGGILRIFPEGKSFIADVEPIFDRLLFFWS-DRRNPH 102
Cdd:smart00702  73 EDAQVARYGP-GGHYGPHVDNFLYGDRIATFILYLND----VEEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLH 147

                           90
                   ....*....|....*...
gi 809281406   103 EVQPSY-ATRYAMTVWYF 119
Cdd:smart00702 148 GVCPVTrGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 24-119 2.69e-31

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: 109.78  E-value: 2.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406    24 HEAMVACYPGnGTGYVRHVDNPNGDGRCITCIYYLNKnwdaKLHGGILRIFPEGKSFIADVEPIFDRLLFFWS-DRRNPH 102
Cdd:smart00702  73 EDAQVARYGP-GGHYGPHVDNFLYGDRIATFILYLND----VEEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLH 147

                           90
                   ....*....|....*...
gi 809281406   103 EVQPSY-ATRYAMTVWYF 119
Cdd:smart00702 148 GVCPVTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
 23-121 3.12e-24

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: 92.31  E-value: 3.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406  23 LHEAMVACYPgNGTGYVRHVD-NPNGDGRCITCIYYLNKNWDAKlHGGILRIFPE-GKSFIADVEPIFDRLLFFWSDRRn 100
Cdd:COG3751   98 EYEGHFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSEEEVTVAPRFNRLVLFLSEEF- 174

                         90       100
                 ....*....|....*....|.
gi 809281406 101 PHEVQPSYATRYAMTVWYFDA 121
Cdd:COG3751  175 PHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 26-119 3.76e-23

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: 86.66  E-value: 3.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406   26 AMVACYpGNGTGYVRHVDN----PNGDGRCITCIYYLNKnWDAKlHGGILRIFPEGKsfIADVEPIFDRLLFFWSDRRNP 101
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLND-WEEE-EGGELVLYDGDG--VEDIKPKKGRLVLFPSSELSL 75

                          90
                  ....*....|....*....
gi 809281406  102 HEVQPSYA-TRYAMTVWYF 119
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 24-119 2.69e-31

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: 109.78  E-value: 2.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406    24 HEAMVACYPGnGTGYVRHVDNPNGDGRCITCIYYLNKnwdaKLHGGILRIFPEGKSFIADVEPIFDRLLFFWS-DRRNPH 102
Cdd:smart00702  73 EDAQVARYGP-GGHYGPHVDNFLYGDRIATFILYLND----VEEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLH 147

                           90
                   ....*....|....*...
gi 809281406   103 EVQPSY-ATRYAMTVWYF 119
Cdd:smart00702 148 GVCPVTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
 23-121 3.12e-24

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: 92.31  E-value: 3.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406  23 LHEAMVACYPgNGTGYVRHVD-NPNGDGRCITCIYYLNKNWDAKlHGGILRIFPE-GKSFIADVEPIFDRLLFFWSDRRn 100
Cdd:COG3751   98 EYEGHFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSEEEVTVAPRFNRLVLFLSEEF- 174

                         90       100
                 ....*....|....*....|.
gi 809281406 101 PHEVQPSYATRYAMTVWYFDA 121
Cdd:COG3751  175 PHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 26-119 3.76e-23

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: 86.66  E-value: 3.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406   26 AMVACYpGNGTGYVRHVDN----PNGDGRCITCIYYLNKnWDAKlHGGILRIFPEGKsfIADVEPIFDRLLFFWSDRRNP 101
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLND-WEEE-EGGELVLYDGDG--VEDIKPKKGRLVLFPSSELSL 75

                          90
                  ....*....|....*....
gi 809281406  102 HEVQPSYA-TRYAMTVWYF 119
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 28-118 3.15e-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: 48.50  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809281406   28 VACYPgNGTGYVRHVDNpnGDGRCITCIYYLNKNWDAKLhGGILRIFP-EGKSFIADVE----PIFDRLLFFwsdRRNP- 101
Cdd:pfam13661   3 CSRYE-KGDFLLCHDDV--IEGRRIAFILYLVENWKPDD-GGALDLYDtDGHGQPADITksivPTWNKLVFF---EVSPg 75

                          90       100
                  ....*....|....*....|..
gi 809281406  102 ---HEVQPSYA--TRYAMTVWY 118
Cdd:pfam13661  76 hsfHQVAEVVAekPRLSISGWF 97
 
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