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Conserved domains on  [gi|221512810|ref|NP_649043|]
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uncharacterized protein Dmel_CG18234 [Drosophila melanogaster]

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 ...
27-159 1.94e-42

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: 147.81  E-value: 1.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810   27 SIAGMKELVDLEGFFISEMESYTAALKNKIDLMESLLQEVQSKREISRRNPEEFVAHPLNAFSLIRRLHEDWTQAELLML 106
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221512810  107 NQVGLEHLQAIETGLE--EAQPSDNDLNDAIGGIISLQQFYNLQPSDIANGLLMG 159
Cdd:pfam08336  81 TNQAVGFLEQLTEMRSrlLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
371-485 2.97e-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: 90.52  E-value: 2.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810   371 RIKDMTG---EDVQEDTDFQIDNYGICGFRNFHTDNielqdqtAELGDRLTSIMFFMNDVAQGGALAFPNLNL----TIW 443
Cdd:smart00702  57 RLADFLGllaGLPLSAEDAQVARYGPGGHYGPHVDN-------FLYGDRIATFILYLNDVEEGGELVFPGLRLmvvaTVK 129
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 221512810   444 PQKGSALVWRNLDHRMqpnqdlLHVSCPVVVGSKWTLVKWLH 485
Cdd:smart00702 130 PKKGDLLFFPSGHGRS------LHGVCPVTRGSRWAITGWIR 165
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
27-159 1.94e-42

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: 147.81  E-value: 1.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810   27 SIAGMKELVDLEGFFISEMESYTAALKNKIDLMESLLQEVQSKREISRRNPEEFVAHPLNAFSLIRRLHEDWTQAELLML 106
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221512810  107 NQVGLEHLQAIETGLE--EAQPSDNDLNDAIGGIISLQQFYNLQPSDIANGLLMG 159
Cdd:pfam08336  81 TNQAVGFLEQLTEMRSrlLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
371-485 2.97e-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: 90.52  E-value: 2.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810   371 RIKDMTG---EDVQEDTDFQIDNYGICGFRNFHTDNielqdqtAELGDRLTSIMFFMNDVAQGGALAFPNLNL----TIW 443
Cdd:smart00702  57 RLADFLGllaGLPLSAEDAQVARYGPGGHYGPHVDN-------FLYGDRIATFILYLNDVEEGGELVFPGLRLmvvaTVK 129
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 221512810   444 PQKGSALVWRNLDHRMqpnqdlLHVSCPVVVGSKWTLVKWLH 485
Cdd:smart00702 130 PKKGDLLFFPSGHGRS------LHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
386-485 6.67e-13

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: 64.32  E-value: 6.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810  386 FQIDNYGICGFRNFHTDNIELQDQTaelGDRLTSIMFFMNDVA--QGGALAFPNLN--LTIWPQKGSALVWRNldhrmqp 461
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGG---GQRRLTVVLYLNDWEeeEGGELVLYDGDgvEDIKPKKGRLVLFPS------- 70
                          90       100
                  ....*....|....*....|....
gi 221512810  462 NQDLLHVSCPVVVGSKWTLVKWLH 485
Cdd:pfam13640  71 SELSLHEVLPVTGGERWSITGWFR 94
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
308-487 5.40e-08

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 54.67  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810 308 KVETLSLKPHIVLYHDVIYDSE------ISKVK--------NISLPSLKSPLRILYAIdynlkFAKIREDHQ-SPLSLRI 372
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAEcdhlvkLAKKKiqrsmvadNKSGKSVMSEVRTSSGM-----FLDKRQDPVvSRIEERI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810 373 KDMTGEDVQEDTDFQIDNYGICGFRNFHTDNIELQDQTAELGDRLTSIMFFMNDVAQGGALAFPNLN------------- 439
Cdd:PLN00052 121 AAWTFLPEENAENIQILRYEHGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfse 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221512810 440 -----LTIWPQKGSALVWRNLDHRMQPNQDLLHVSCPVVVGSKWTLVKWLHER 487
Cdd:PLN00052 201 cahkgLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIR 253
 
Name Accession Description Interval E-value
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
27-159 1.94e-42

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: 147.81  E-value: 1.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810   27 SIAGMKELVDLEGFFISEMESYTAALKNKIDLMESLLQEVQSKREISRRNPEEFVAHPLNAFSLIRRLHEDWTQAELLML 106
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLSNPLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 221512810  107 NQVGLEHLQAIETGLE--EAQPSDNDLNDAIGGIISLQQFYNLQPSDIANGLLMG 159
Cdd:pfam08336  81 TNQAVGFLEQLTEMRSrlLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
371-485 2.97e-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: 90.52  E-value: 2.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810   371 RIKDMTG---EDVQEDTDFQIDNYGICGFRNFHTDNielqdqtAELGDRLTSIMFFMNDVAQGGALAFPNLNL----TIW 443
Cdd:smart00702  57 RLADFLGllaGLPLSAEDAQVARYGPGGHYGPHVDN-------FLYGDRIATFILYLNDVEEGGELVFPGLRLmvvaTVK 129
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 221512810   444 PQKGSALVWRNLDHRMqpnqdlLHVSCPVVVGSKWTLVKWLH 485
Cdd:smart00702 130 PKKGDLLFFPSGHGRS------LHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
386-485 6.67e-13

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: 64.32  E-value: 6.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810  386 FQIDNYGICGFRNFHTDNIELQDQTaelGDRLTSIMFFMNDVA--QGGALAFPNLN--LTIWPQKGSALVWRNldhrmqp 461
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGG---GQRRLTVVLYLNDWEeeEGGELVLYDGDgvEDIKPKKGRLVLFPS------- 70
                          90       100
                  ....*....|....*....|....
gi 221512810  462 NQDLLHVSCPVVVGSKWTLVKWLH 485
Cdd:pfam13640  71 SELSLHEVLPVTGGERWSITGWFR 94
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
308-487 5.40e-08

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 54.67  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810 308 KVETLSLKPHIVLYHDVIYDSE------ISKVK--------NISLPSLKSPLRILYAIdynlkFAKIREDHQ-SPLSLRI 372
Cdd:PLN00052  46 RVKAVSWQPRIFVYKGFLSDAEcdhlvkLAKKKiqrsmvadNKSGKSVMSEVRTSSGM-----FLDKRQDPVvSRIEERI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221512810 373 KDMTGEDVQEDTDFQIDNYGICGFRNFHTDNIELQDQTAELGDRLTSIMFFMNDVAQGGALAFPNLN------------- 439
Cdd:PLN00052 121 AAWTFLPEENAENIQILRYEHGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfse 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221512810 440 -----LTIWPQKGSALVWRNLDHRMQPNQDLLHVSCPVVVGSKWTLVKWLHER 487
Cdd:PLN00052 201 cahkgLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIR 253
 
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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