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Conserved domains on  [gi|226371643|ref|NP_001139761|]
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prolyl 3-hydroxylase 1 isoform 2 precursor [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

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List of domain hits

Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
479-677 1.11e-34

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: 129.43  E-value: 1.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643   479 SDHECQELQRLTNVAATSGDGYRGQTSP-HTPNEKFYGVTVFKALKlgqegkvplqsahlYYNVTEKVRRIMESYFrldt 557
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643   558 PLYFSYSHLVCRTAIEEVQaerKDDSHPVHVDNCilnaetlvcvkeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 637
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 226371643   638 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 677
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
479-677 1.11e-34

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: 129.43  E-value: 1.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643   479 SDHECQELQRLTNVAATSGDGYRGQTSP-HTPNEKFYGVTVFKALKlgqegkvplqsahlYYNVTEKVRRIMESYFrldt 557
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643   558 PLYFSYSHLVCRTAIEEVQaerKDDSHPVHVDNCilnaetlvcvkeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 637
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 226371643   638 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 677
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
586-676 2.75e-12

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: 63.16  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643  586 VHVDNCILNAETLvcvkeppaytFRDYSAILYLNG--DFDGGNFyftELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKA 663
Cdd:pfam13640  14 PHLDFFEGAEGGG----------QRRLTVVLYLNDweEEEGGEL---VLYDGDGVEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 226371643  664 VTRGQRCAIALWF 676
Cdd:pfam13640  81 VTGGERWSITGWF 93
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
479-677 1.11e-34

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: 129.43  E-value: 1.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643   479 SDHECQELQRLTNVAATSGDGYRGQTSP-HTPNEKFYGVTVFKALKlgqegkvplqsahlYYNVTEKVRRIMESYFrldt 557
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643   558 PLYFSYSHLVCRTAIEEVQaerKDDSHPVHVDNCilnaetlvcvkeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 637
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 226371643   638 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 677
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
586-676 2.75e-12

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: 63.16  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371643  586 VHVDNCILNAETLvcvkeppaytFRDYSAILYLNG--DFDGGNFyftELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKA 663
Cdd:pfam13640  14 PHLDFFEGAEGGG----------QRRLTVVLYLNDweEEEGGEL---VLYDGDGVEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 226371643  664 VTRGQRCAIALWF 676
Cdd:pfam13640  81 VTGGERWSITGWF 93
 
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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