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Conserved domains on  [gi|116008537|ref|NP_733379|]
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uncharacterized protein Dmel_CG31524, isoform A [Drosophila melanogaster]

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

 Zoom to residue level

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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 ...
340-507 2.60e-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: 127.12  E-value: 2.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   340 KEGALIRSSSKNQILPSETVNA-ANEFEIAKFRTSKSVWFD-SDANEATLKLTQRLGEATGL---DMKHSEPFQVINYGI 414
Cdd:smart00702   3 AECQKLLEEAEPLGWRGEVTRGiGNPNETSQYRQSNGTWLElLERDLVIERIRQRLADFLGLlagLPLSAEDAQVARYGP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   415 GGVFESHFDtsladedRFVNGyiDRLATTLFYLNDVPQGGATHFPGLNI----TVFPKFGTVLMWYNLHTegmlhvRTMH 490
Cdd:smart00702  83 GGHYGPHVD-------NFLYG--DRIATFILYLNDVEEGGELVFPGLRLmvvaTVKPKKGDLLFFPSGHG------RSLH 147
                          170
                   ....*....|....*..
gi 116008537   491 TGCPVIVGSKWVVSKWI 507
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
31-159 6.41e-30

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: 113.91  E-value: 6.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   31 SVVNMDDLLNMEDDLVSKLEGYAEKLSYKANTIRWGIQQMREQLDKSKKEQSFDL---FNRYSFIRHMQADWLMWKQYLD 107
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLsnpLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116008537  108 KPV---IRDELNYKQMDNLRMPQELDLFDASEAIRRMQATYAMLSNDIAEGFLDG 159
Cdd:pfam08336  81 TNQavgFLEQLTEMRSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
172-256 1.91e-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: 38.63  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 172 LAMGRHLMNQSRWTIAEQWILAGIKAQdrkgpqtemillrgPTKAELFRTLGKVRFERRNEEGALKAYQAALKHSPHDLE 251
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELD--------------PDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE 73

                 ....*
gi 116008537 252 IFQEY 256
Cdd:COG4783   74 ARLNL 78
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
340-507 2.60e-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: 127.12  E-value: 2.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   340 KEGALIRSSSKNQILPSETVNA-ANEFEIAKFRTSKSVWFD-SDANEATLKLTQRLGEATGL---DMKHSEPFQVINYGI 414
Cdd:smart00702   3 AECQKLLEEAEPLGWRGEVTRGiGNPNETSQYRQSNGTWLElLERDLVIERIRQRLADFLGLlagLPLSAEDAQVARYGP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   415 GGVFESHFDtsladedRFVNGyiDRLATTLFYLNDVPQGGATHFPGLNI----TVFPKFGTVLMWYNLHTegmlhvRTMH 490
Cdd:smart00702  83 GGHYGPHVD-------NFLYG--DRIATFILYLNDVEEGGELVFPGLRLmvvaTVKPKKGDLLFFPSGHG------RSLH 147
                          170
                   ....*....|....*..
gi 116008537   491 TGCPVIVGSKWVVSKWI 507
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
31-159 6.41e-30

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: 113.91  E-value: 6.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   31 SVVNMDDLLNMEDDLVSKLEGYAEKLSYKANTIRWGIQQMREQLDKSKKEQSFDL---FNRYSFIRHMQADWLMWKQYLD 107
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLsnpLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116008537  108 KPV---IRDELNYKQMDNLRMPQELDLFDASEAIRRMQATYAMLSNDIAEGFLDG 159
Cdd:pfam08336  81 TNQavgFLEQLTEMRSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
407-507 7.96e-17

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: 75.88  E-value: 7.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537  407 FQVINYGIGGVFESHFDTSLADEdrfvnGYIDRLATTLFYLNDVP--QGGAT--HFPGLNITVFPKFGTVLMWYNlhteg 482
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE-----GGGQRRLTVVLYLNDWEeeEGGELvlYDGDGVEDIKPKKGRLVLFPS----- 70
                          90       100
                  ....*....|....*....|....*
gi 116008537  483 mlHVRTMHTGCPVIVGSKWVVSKWI 507
Cdd:pfam13640  71 --SELSLHEVLPVTGGERWSITGWF 93
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
360-513 1.88e-16

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 80.10  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 360 NAANEFEIAKFRTSKSVWFDSDANEATLKLTQRLGEATGLDMKHSEPFQVINYGIGGVFESHFDTSLADEDRFVNGYidR 439
Cdd:PLN00052  87 NKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAENIQILRYEHGQKYEPHFDYFHDKINQALGGH--R 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 440 LATTLFYLNDVPQGGATHFPGLN------------------ITVFPKFGTVLMWYNLHTEGMLHVRTMHTGCPVIVGSKW 501
Cdd:PLN00052 165 YATVLMYLSTVDKGGETVFPNAEgwenqpkddtfsecahkgLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKW 244
                        170
                 ....*....|..
gi 116008537 502 VVSKWIDDKGQE 513
Cdd:PLN00052 245 SAPKWIHIRSYE 256
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
172-256 1.91e-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: 38.63  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 172 LAMGRHLMNQSRWTIAEQWILAGIKAQdrkgpqtemillrgPTKAELFRTLGKVRFERRNEEGALKAYQAALKHSPHDLE 251
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELD--------------PDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE 73

                 ....*
gi 116008537 252 IFQEY 256
Cdd:COG4783   74 ARLNL 78
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
340-507 2.60e-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: 127.12  E-value: 2.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   340 KEGALIRSSSKNQILPSETVNA-ANEFEIAKFRTSKSVWFD-SDANEATLKLTQRLGEATGL---DMKHSEPFQVINYGI 414
Cdd:smart00702   3 AECQKLLEEAEPLGWRGEVTRGiGNPNETSQYRQSNGTWLElLERDLVIERIRQRLADFLGLlagLPLSAEDAQVARYGP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   415 GGVFESHFDtsladedRFVNGyiDRLATTLFYLNDVPQGGATHFPGLNI----TVFPKFGTVLMWYNLHTegmlhvRTMH 490
Cdd:smart00702  83 GGHYGPHVD-------NFLYG--DRIATFILYLNDVEEGGELVFPGLRLmvvaTVKPKKGDLLFFPSGHG------RSLH 147
                          170
                   ....*....|....*..
gi 116008537   491 TGCPVIVGSKWVVSKWI 507
Cdd:smart00702 148 GVCPVTRGSRWAITGWI 164
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
31-159 6.41e-30

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: 113.91  E-value: 6.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537   31 SVVNMDDLLNMEDDLVSKLEGYAEKLSYKANTIRWGIQQMREQLDKSKKEQSFDL---FNRYSFIRHMQADWLMWKQYLD 107
Cdd:pfam08336   1 SVSGLEKLLELERELIDNLENYIEELEEKLDTLKRFLEELKREHEKADEDPEEYLsnpLNAFSLIKRLHQDWPKWEKLMK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116008537  108 KPV---IRDELNYKQMDNLRMPQELDLFDASEAIRRMQATYAMLSNDIAEGFLDG 159
Cdd:pfam08336  81 TNQavgFLEQLTEMRSRLLKLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
407-507 7.96e-17

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: 75.88  E-value: 7.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537  407 FQVINYGIGGVFESHFDTSLADEdrfvnGYIDRLATTLFYLNDVP--QGGAT--HFPGLNITVFPKFGTVLMWYNlhteg 482
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE-----GGGQRRLTVVLYLNDWEeeEGGELvlYDGDGVEDIKPKKGRLVLFPS----- 70
                          90       100
                  ....*....|....*....|....*
gi 116008537  483 mlHVRTMHTGCPVIVGSKWVVSKWI 507
Cdd:pfam13640  71 --SELSLHEVLPVTGGERWSITGWF 93
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
360-513 1.88e-16

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 80.10  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 360 NAANEFEIAKFRTSKSVWFDSDANEATLKLTQRLGEATGLDMKHSEPFQVINYGIGGVFESHFDTSLADEDRFVNGYidR 439
Cdd:PLN00052  87 NKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAENIQILRYEHGQKYEPHFDYFHDKINQALGGH--R 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 440 LATTLFYLNDVPQGGATHFPGLN------------------ITVFPKFGTVLMWYNLHTEGMLHVRTMHTGCPVIVGSKW 501
Cdd:PLN00052 165 YATVLMYLSTVDKGGETVFPNAEgwenqpkddtfsecahkgLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKW 244
                        170
                 ....*....|..
gi 116008537 502 VVSKWIDDKGQE 513
Cdd:PLN00052 245 SAPKWIHIRSYE 256
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
172-256 1.91e-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: 38.63  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 172 LAMGRHLMNQSRWTIAEQWILAGIKAQdrkgpqtemillrgPTKAELFRTLGKVRFERRNEEGALKAYQAALKHSPHDLE 251
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELD--------------PDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE 73

                 ....*
gi 116008537 252 IFQEY 256
Cdd:COG4783   74 ARLNL 78
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
171-263 7.79e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.21  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008537 171 CLAMGRHLMNQSRWTIAEQWILAGIKAQdrkgpqtemillrgPTKAELFRTLGKVRFERRNEEGALKAYQAALKHSPHDL 250
Cdd:COG3914  149 YLNLGEALRRLGRLEEAIAALRRALELD--------------PDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214
                         90
                 ....*....|...
gi 116008537 251 EIFQEYQNLKRRV 263
Cdd:COG3914  215 DAHSNLLFALRQA 227
 
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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