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Conserved domains on  [gi|570700854|ref|NP_001275677|]
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prolyl 4-hydroxylase subunit alpha-3 isoform 2 precursor [Homo sapiens]

Protein Classification

prolyl 4-hydroxylase( domain architecture ID 20591303)

prolyl 4-hydroxylase catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins

CATH:  2.60.120.620
EC:  1.14.11.2
Gene Ontology:  GO:0004656|GO:0005506

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 58-160 7.25e-27

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


:

Pssm-ID: 462433  Cd Length: 135  Bit Score: 105.82  E-value: 7.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854   58 EEARLRDLTRFYDKVLSLH----EDSTTPVANPLLAFTLIKRLQSDWR---NVVHSLEASENIRALKDGYEKVEQdLPAF 130
Cdd:pfam08336  26 LEEKLDTLKRFLEELKREHekadEDPEEYLSNPLNAFSLIKRLHQDWPkweKLMKTNQAVGFLEQLTEMRSRLLK-LPTD 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 570700854  131 EDLEGAARALMRLQDVYMLNVKGLARGVFQ 160
Cdd:pfam08336 105 EDLEGAAEALLRLQDTYNLDPSDLANGNLN 134
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 356-478 1.84e-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: 1.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854   356 SDSEAQKIRELAEPWLQRSVVASG--EKQLQVEYRISKSAWLK-DTVDPKLVTLNHRIAALTGLDVR-PPYAEYLQVVNY 431
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGigNPNETSQYRQSNGTWLElLERDLVIERIRQRLADFLGLLAGlPLSAEDAQVARY 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 570700854   432 GIGGHYEPHFDHATSpssplyrmksGNRVATFMIYLSSVEAGGATAF 478
Cdd:smart00702  81 GPGGHYGPHVDNFLY----------GDRIATFILYLNDVEEGGELVF 117
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 188-289 3.69e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854 188 GKVAYDMGDYYHAIPWLEEAVSLFRGSYgewktedeasleDALDHLAFAYFRAGNVSCALSLSREFLLYSPDNkrmARNV 267
Cdd:COG4783   45 GEILLQLGDLDEAIVLLHEALELDPDEP------------EARLNLGLALLKAGDYDEALALLEKALKLDPEH---PEAY 109

                         90       100
                 ....*....|....*....|..
gi 570700854 268 LKYERLLAESPNHVVAEAVIQR 289
Cdd:COG4783  110 LRLARAYRALGRPDEAIAALEK 131
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 58-160 7.25e-27

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 105.82  E-value: 7.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854   58 EEARLRDLTRFYDKVLSLH----EDSTTPVANPLLAFTLIKRLQSDWR---NVVHSLEASENIRALKDGYEKVEQdLPAF 130
Cdd:pfam08336  26 LEEKLDTLKRFLEELKREHekadEDPEEYLSNPLNAFSLIKRLHQDWPkweKLMKTNQAVGFLEQLTEMRSRLLK-LPTD 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 570700854  131 EDLEGAARALMRLQDVYMLNVKGLARGVFQ 160
Cdd:pfam08336 105 EDLEGAAEALLRLQDTYNLDPSDLANGNLN 134
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 356-478 1.84e-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: 1.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854   356 SDSEAQKIRELAEPWLQRSVVASG--EKQLQVEYRISKSAWLK-DTVDPKLVTLNHRIAALTGLDVR-PPYAEYLQVVNY 431
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGigNPNETSQYRQSNGTWLElLERDLVIERIRQRLADFLGLLAGlPLSAEDAQVARY 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 570700854   432 GIGGHYEPHFDHATSpssplyrmksGNRVATFMIYLSSVEAGGATAF 478
Cdd:smart00702  81 GPGGHYGPHVDNFLY----------GDRIATFILYLNDVEEGGELVF 117
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 338-478 1.52e-18

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 86.65  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854 338 RKEVIHLEPYIALYHDFVSDSEAQKIRELAEPWLQRSVVASGE--KQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTG 415
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKsgKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTF 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570700854 416 LDvrPPYAEYLQVVNYGIGGHYEPHFDHAtspSSPLYRMKSGNRVATFMIYLSSVEAGGATAF 478
Cdd:PLN00052 126 LP--EENAENIQILRYEHGQKYEPHFDYF---HDKINQALGGHRYATVLMYLSTVDKGGETVF 183
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 426-478 1.07e-06

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: 46.99  E-value: 1.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 570700854  426 LQVVNYGIGGHYEPHFDHATSPSSplyrmkSGNRVATFMIYLSSV--EAGGATAF 478
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEG------GGQRRLTVVLYLNDWeeEEGGELVL 49
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 188-289 3.69e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854 188 GKVAYDMGDYYHAIPWLEEAVSLFRGSYgewktedeasleDALDHLAFAYFRAGNVSCALSLSREFLLYSPDNkrmARNV 267
Cdd:COG4783   45 GEILLQLGDLDEAIVLLHEALELDPDEP------------EARLNLGLALLKAGDYDEALALLEKALKLDPEH---PEAY 109

                         90       100
                 ....*....|....*....|..
gi 570700854 268 LKYERLLAESPNHVVAEAVIQR 289
Cdd:COG4783  110 LRLARAYRALGRPDEAIAALEK 131
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 58-160 7.25e-27

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 105.82  E-value: 7.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854   58 EEARLRDLTRFYDKVLSLH----EDSTTPVANPLLAFTLIKRLQSDWR---NVVHSLEASENIRALKDGYEKVEQdLPAF 130
Cdd:pfam08336  26 LEEKLDTLKRFLEELKREHekadEDPEEYLSNPLNAFSLIKRLHQDWPkweKLMKTNQAVGFLEQLTEMRSRLLK-LPTD 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 570700854  131 EDLEGAARALMRLQDVYMLNVKGLARGVFQ 160
Cdd:pfam08336 105 EDLEGAAEALLRLQDTYNLDPSDLANGNLN 134
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 356-478 1.84e-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: 1.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854   356 SDSEAQKIRELAEPWLQRSVVASG--EKQLQVEYRISKSAWLK-DTVDPKLVTLNHRIAALTGLDVR-PPYAEYLQVVNY 431
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGigNPNETSQYRQSNGTWLElLERDLVIERIRQRLADFLGLLAGlPLSAEDAQVARY 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 570700854   432 GIGGHYEPHFDHATSpssplyrmksGNRVATFMIYLSSVEAGGATAF 478
Cdd:smart00702  81 GPGGHYGPHVDNFLY----------GDRIATFILYLNDVEEGGELVF 117
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 338-478 1.52e-18

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 86.65  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854 338 RKEVIHLEPYIALYHDFVSDSEAQKIRELAEPWLQRSVVASGE--KQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTG 415
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKsgKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTF 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570700854 416 LDvrPPYAEYLQVVNYGIGGHYEPHFDHAtspSSPLYRMKSGNRVATFMIYLSSVEAGGATAF 478
Cdd:PLN00052 126 LP--EENAENIQILRYEHGQKYEPHFDYF---HDKINQALGGHRYATVLMYLSTVDKGGETVF 183
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 426-478 1.07e-06

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: 46.99  E-value: 1.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 570700854  426 LQVVNYGIGGHYEPHFDHATSPSSplyrmkSGNRVATFMIYLSSV--EAGGATAF 478
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEG------GGQRRLTVVLYLNDWeeEEGGELVL 49
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 188-289 3.69e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570700854 188 GKVAYDMGDYYHAIPWLEEAVSLFRGSYgewktedeasleDALDHLAFAYFRAGNVSCALSLSREFLLYSPDNkrmARNV 267
Cdd:COG4783   45 GEILLQLGDLDEAIVLLHEALELDPDEP------------EARLNLGLALLKAGDYDEALALLEKALKLDPEH---PEAY 109

                         90       100
                 ....*....|....*....|..
gi 570700854 268 LKYERLLAESPNHVVAEAVIQR 289
Cdd:COG4783  110 LRLARAYRALGRPDEAIAALEK 131
 
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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