NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1000743496|ref|XP_015594433|]
View 

prolyl 3-hydroxylase 2 [Cephus cinctus]

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 ...
 542-690 4.29e-20

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: 87.83  E-value: 4.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496  542 LVEPELLDLVLrstEAARDHLERYLhldqQLHFTYTHLVCRSALLDTSSDrerLSHAIHADNCLlddqnncirkspaYTW 621
Cdd:smart00702  41 WLELLERDLVI---ERIRQRLADFL----GLLAGLPLSAEDAQVARYGPG---GHYGPHVDNFL-------------YGD 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496  622 RDYSAILYLNDDFSGGEFIFAKTQTMesIQSTVQPRCGRMVGF-SADGNNLHGVRGILRGKRCALALWFT 690
Cdd:smart00702  98 RIATFILYLNDVEEGGELVFPGLRLM--VVATVKPKKGDLLFFpSGHGRSLHGVCPVTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 542-690 4.29e-20

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: 87.83  E-value: 4.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496  542 LVEPELLDLVLrstEAARDHLERYLhldqQLHFTYTHLVCRSALLDTSSDrerLSHAIHADNCLlddqnncirkspaYTW 621
Cdd:smart00702  41 WLELLERDLVI---ERIRQRLADFL----GLLAGLPLSAEDAQVARYGPG---GHYGPHVDNFL-------------YGD 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496  622 RDYSAILYLNDDFSGGEFIFAKTQTMesIQSTVQPRCGRMVGF-SADGNNLHGVRGILRGKRCALALWFT 690
Cdd:smart00702  98 RIATFILYLNDVEEGGELVFPGLRLM--VVATVKPKKGDLLFFpSGHGRSLHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 599-689 1.30e-10

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: 58.54  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496 599 IHADNCLLDDQNNcirkspaytWRDYSAILYLND--DFSGGEFIFAKTQTMESIQstvqPRCGRMVGFSADGNNLHGVRG 676
Cdd:pfam13640  14 PHLDFFEGAEGGG---------QRRLTVVLYLNDweEEEGGELVLYDGDGVEDIK----PKKGRLVLFPSSELSLHEVLP 80

                          90
                  ....*....|...
gi 1000743496 677 ILRGKRCALALWF 689
Cdd:pfam13640  81 VTGGERWSITGWF 93
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
 621-689 4.14e-05

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: 44.93  E-value: 4.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1000743496 621 WRDYSAILYLNDD---FSGGEFIFAKTQtMESIQSTVQPRCGRMVGFSADgNNLHGVRgILRGKRCALALWF 689
Cdd:COG3751   124 NRRLSLVLYLNPDwqpEWGGELELYDDD-GSEEEVTVAPRFNRLVLFLSE-EFPHEVL-PVGRERLSIAGWF 192
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 542-690 4.29e-20

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: 87.83  E-value: 4.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496  542 LVEPELLDLVLrstEAARDHLERYLhldqQLHFTYTHLVCRSALLDTSSDrerLSHAIHADNCLlddqnncirkspaYTW 621
Cdd:smart00702  41 WLELLERDLVI---ERIRQRLADFL----GLLAGLPLSAEDAQVARYGPG---GHYGPHVDNFL-------------YGD 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496  622 RDYSAILYLNDDFSGGEFIFAKTQTMesIQSTVQPRCGRMVGF-SADGNNLHGVRGILRGKRCALALWFT 690
Cdd:smart00702  98 RIATFILYLNDVEEGGELVFPGLRLM--VVATVKPKKGDLLFFpSGHGRSLHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 599-689 1.30e-10

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: 58.54  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000743496 599 IHADNCLLDDQNNcirkspaytWRDYSAILYLND--DFSGGEFIFAKTQTMESIQstvqPRCGRMVGFSADGNNLHGVRG 676
Cdd:pfam13640  14 PHLDFFEGAEGGG---------QRRLTVVLYLNDweEEEGGELVLYDGDGVEDIK----PKKGRLVLFPSSELSLHEVLP 80

                          90
                  ....*....|...
gi 1000743496 677 ILRGKRCALALWF 689
Cdd:pfam13640  81 VTGGERWSITGWF 93
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
 621-689 4.14e-05

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: 44.93  E-value: 4.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1000743496 621 WRDYSAILYLNDD---FSGGEFIFAKTQtMESIQSTVQPRCGRMVGFSADgNNLHGVRgILRGKRCALALWF 689
Cdd:COG3751   124 NRRLSLVLYLNPDwqpEWGGELELYDDD-GSEEEVTVAPRFNRLVLFLSE-EFPHEVL-PVGRERLSIAGWF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH