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Conserved domains on  [gi|63252888|ref|NP_001017962|]
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prolyl 4-hydroxylase subunit alpha-1 isoform 2 precursor [Homo sapiens]

Protein Classification

prolyl 4-hydroxylase subunit alpha( domain architecture ID 10551047)

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:0031418|GO:0005506
PubMed:  20199358|23489300

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 ...
24-155 1.39e-52

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: 175.15  E-value: 1.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    24 SIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVL 103
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63252888   104 KDMSDGFISNLTIQRQY---FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPG 155
Cdd:pfam08336  81 TNQAVGFLEQLTEMRSRllkLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
345-518 2.22e-52

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: 175.65  E-value: 2.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    345 SDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYE-NPVVSRINMRIQDLTGL---DVSTAEELQVANY 420
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYRQSNGTWLELLErDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    421 GVGGQYEPHFDFARKdepdafkelgtGNRIATWLFYMSDVSAGGATVFPE----VGASVWPKKGTAVFWYNlfasgeGDY 496
Cdd:smart00702  81 GPGGHYGPHVDNFLY-----------GDRIATFILYLNDVEEGGELVFPGlrlmVVATVKPKKGDLLFFPS------GHG 143
                          170       180
                   ....*....|....*....|..
gi 63252888    497 STRHAACPVLVGNKWVSNKWLH 518
Cdd:smart00702 144 RSLHGVCPVTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
24-155 1.39e-52

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: 175.15  E-value: 1.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    24 SIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVL 103
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63252888   104 KDMSDGFISNLTIQRQY---FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPG 155
Cdd:pfam08336  81 TNQAVGFLEQLTEMRSRllkLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
345-518 2.22e-52

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: 175.65  E-value: 2.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    345 SDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYE-NPVVSRINMRIQDLTGL---DVSTAEELQVANY 420
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYRQSNGTWLELLErDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    421 GVGGQYEPHFDFARKdepdafkelgtGNRIATWLFYMSDVSAGGATVFPE----VGASVWPKKGTAVFWYNlfasgeGDY 496
Cdd:smart00702  81 GPGGHYGPHVDNFLY-----------GDRIATFILYLNDVEEGGELVFPGlrlmVVATVKPKKGDLLFFPS------GHG 143
                          170       180
                   ....*....|....*....|..
gi 63252888    497 STRHAACPVLVGNKWVSNKWLH 518
Cdd:smart00702 144 RSLHGVCPVTRGSRWAITGWIR 165
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
334-523 9.27e-34

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 130.17  E-value: 9.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888  334 KPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAE 413
Cdd:PLN00052  53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888  414 ELQVANYGVGGQYEPHFDFARkdepDAFKELGTGNRIATWLFYMSDVSAGGATVFPEV------------------GASV 475
Cdd:PLN00052 133 NIQILRYEHGQKYEPHFDYFH----DKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwenqpkddtfsecahkGLAV 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 63252888  476 WPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQE 523
Cdd:PLN00052 209 KPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYE 256
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
415-518 2.90e-20

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: 85.51  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888   415 LQVANYGVGGQYEPHFDFARKDEpdafkelGTGNRIATWLFYMSDVSA--GGATVF--PEVGASVWPKKGTAVFWYNlfa 490
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE-------GGGQRRLTVVLYLNDWEEeeGGELVLydGDGVEDIKPKKGRLVLFPS--- 70
                          90       100
                  ....*....|....*....|....*...
gi 63252888   491 sgegDYSTRHAACPVLVGNKWVSNKWLH 518
Cdd:pfam13640  71 ----SELSLHEVLPVTGGERWSITGWFR 94
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
24-155 1.39e-52

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: 175.15  E-value: 1.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    24 SIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVL 103
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63252888   104 KDMSDGFISNLTIQRQY---FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPG 155
Cdd:pfam08336  81 TNQAVGFLEQLTEMRSRllkLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
345-518 2.22e-52

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: 175.65  E-value: 2.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    345 SDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYE-NPVVSRINMRIQDLTGL---DVSTAEELQVANY 420
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYRQSNGTWLELLErDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888    421 GVGGQYEPHFDFARKdepdafkelgtGNRIATWLFYMSDVSAGGATVFPE----VGASVWPKKGTAVFWYNlfasgeGDY 496
Cdd:smart00702  81 GPGGHYGPHVDNFLY-----------GDRIATFILYLNDVEEGGELVFPGlrlmVVATVKPKKGDLLFFPS------GHG 143
                          170       180
                   ....*....|....*....|..
gi 63252888    497 STRHAACPVLVGNKWVSNKWLH 518
Cdd:smart00702 144 RSLHGVCPVTRGSRWAITGWIR 165
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
334-523 9.27e-34

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 130.17  E-value: 9.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888  334 KPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAE 413
Cdd:PLN00052  53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888  414 ELQVANYGVGGQYEPHFDFARkdepDAFKELGTGNRIATWLFYMSDVSAGGATVFPEV------------------GASV 475
Cdd:PLN00052 133 NIQILRYEHGQKYEPHFDYFH----DKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwenqpkddtfsecahkGLAV 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 63252888  476 WPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQE 523
Cdd:PLN00052 209 KPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYE 256
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
415-518 2.90e-20

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: 85.51  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888   415 LQVANYGVGGQYEPHFDFARKDEpdafkelGTGNRIATWLFYMSDVSA--GGATVF--PEVGASVWPKKGTAVFWYNlfa 490
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE-------GGGQRRLTVVLYLNDWEEeeGGELVLydGDGVEDIKPKKGRLVLFPS--- 70
                          90       100
                  ....*....|....*....|....*...
gi 63252888   491 sgegDYSTRHAACPVLVGNKWVSNKWLH 518
Cdd:pfam13640  71 ----SELSLHEVLPVTGGERWSITGWFR 94
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
412-519 2.13e-07

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.


Pssm-ID: 397334 [Multi-domain]  Cd Length: 101  Bit Score: 48.99  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63252888   412 AEELQVANYgvggqYEPHfdfarkdePDAFKELGTG-NRIATWLFYMSDVSAGGATVF--------PEVGASVWPKKGTA 482
Cdd:pfam03171   1 PDQCLVLNY-----YPPH--------PDPDLTLGLGpHTDASILTILLQDDVGGLQVFkdgkwidvPPLPGALVVNIGDQ 67
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 63252888   483 V-FWYNLFasgegDYSTRHAACPVLVG-NKWVSNKWLHE 519
Cdd:pfam03171  68 LeLLSNGR-----YKSVLHRVLPVNKGkERISIAFFLRP 101
 
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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