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Conserved domains on  [gi|109150439|ref|NP_001035874|]
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prolyl 3-hydroxylase 1 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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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 ...
303-501 6.16e-36

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: 131.74  E-value: 6.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439   303 SDDECQELQRLTNAAATSGDGYRGQTSP-HTPNEKFYGVTVLKALKlgqegkvplqsarmYYNVTEKVRRVMESYFrldt 381
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439   382 PLYFSYSHLVCRTAIEESQaerKDSSHPVHVDNCilnaealmcikeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 461
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 109150439   462 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 501
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
24-204 2.09e-03

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


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  24 LEAKPHMHE--FRLGVRLYSEEKPQEAVPHLEAALQEyfvadeecralceGPYDYDGYNYLD---YSADLFQAITDHYVQ 98
Cdd:COG3914  105 LALNPDNAEalFNLGNLLLALGRLEEALAALRRALAL-------------NPDFAEAYLNLGealRRLGRLEEAIAALRR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  99 VLnckqncvtelashpsREKPfeDFLPSHYNyLQFAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYytAMLGEEEAS 178
Cdd:COG3914  172 AL---------------ELDP--DNAEALNN-LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLF--ALRQACDWE 231
                        170       180
                 ....*....|....*....|....*.
gi 109150439 179 SISPRENAEEYRRRSLLEKELLFFAY 204
Cdd:COG3914  232 VYDRFEELLAALARGPSELSPFALLY 257
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
303-501 6.16e-36

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: 131.74  E-value: 6.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439   303 SDDECQELQRLTNAAATSGDGYRGQTSP-HTPNEKFYGVTVLKALKlgqegkvplqsarmYYNVTEKVRRVMESYFrldt 381
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439   382 PLYFSYSHLVCRTAIEESQaerKDSSHPVHVDNCilnaealmcikeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 461
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 109150439   462 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 501
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
410-500 1.24e-12

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: 63.93  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  410 VHVDNCILNAEALmcikeppaytFRDYSAILYLNG--DFDGGNFyftELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKA 487
Cdd:pfam13640  14 PHLDFFEGAEGGG----------QRRLTVVLYLNDweEEEGGEL---VLYDGDGVEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 109150439  488 VTRGQRCAIALWF 500
Cdd:pfam13640  81 VTGGERWSITGWF 93
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
24-204 2.09e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  24 LEAKPHMHE--FRLGVRLYSEEKPQEAVPHLEAALQEyfvadeecralceGPYDYDGYNYLD---YSADLFQAITDHYVQ 98
Cdd:COG3914  105 LALNPDNAEalFNLGNLLLALGRLEEALAALRRALAL-------------NPDFAEAYLNLGealRRLGRLEEAIAALRR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  99 VLnckqncvtelashpsREKPfeDFLPSHYNyLQFAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYytAMLGEEEAS 178
Cdd:COG3914  172 AL---------------ELDP--DNAEALNN-LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLF--ALRQACDWE 231
                        170       180
                 ....*....|....*....|....*.
gi 109150439 179 SISPRENAEEYRRRSLLEKELLFFAY 204
Cdd:COG3914  232 VYDRFEELLAALARGPSELSPFALLY 257
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
303-501 6.16e-36

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: 131.74  E-value: 6.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439   303 SDDECQELQRLTNAAATSGDGYRGQTSP-HTPNEKFYGVTVLKALKlgqegkvplqsarmYYNVTEKVRRVMESYFrldt 381
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439   382 PLYFSYSHLVCRTAIEESQaerKDSSHPVHVDNCilnaealmcikeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 461
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 109150439   462 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 501
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
410-500 1.24e-12

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: 63.93  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  410 VHVDNCILNAEALmcikeppaytFRDYSAILYLNG--DFDGGNFyftELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKA 487
Cdd:pfam13640  14 PHLDFFEGAEGGG----------QRRLTVVLYLNDweEEEGGEL---VLYDGDGVEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 109150439  488 VTRGQRCAIALWF 500
Cdd:pfam13640  81 VTGGERWSITGWF 93
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
24-204 2.09e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  24 LEAKPHMHE--FRLGVRLYSEEKPQEAVPHLEAALQEyfvadeecralceGPYDYDGYNYLD---YSADLFQAITDHYVQ 98
Cdd:COG3914  105 LALNPDNAEalFNLGNLLLALGRLEEALAALRRALAL-------------NPDFAEAYLNLGealRRLGRLEEAIAALRR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  99 VLnckqncvtelashpsREKPfeDFLPSHYNyLQFAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYytAMLGEEEAS 178
Cdd:COG3914  172 AL---------------ELDP--DNAEALNN-LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLF--ALRQACDWE 231
                        170       180
                 ....*....|....*....|....*.
gi 109150439 179 SISPRENAEEYRRRSLLEKELLFFAY 204
Cdd:COG3914  232 VYDRFEELLAALARGPSELSPFALLY 257
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
18-177 4.45e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.98  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  18 EADFRDLEAKPHMHEFRLGVRLYSEEKPQEAVPHLEAALQEYfvadeecralcegPYDYDGYNYLdysADLFQAItDHYV 97
Cdd:COG3914   67 AAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN-------------PDNAEALFNL---GNLLLAL-GRLE 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150439  98 QVLNCKQNCvteLASHPsrekpfeDFLPSHYNYLQfAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYYTAMLGE-EE 176
Cdd:COG3914  130 EALAALRRA---LALNP-------DFAEAYLNLGE-ALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRlEE 198

                 .
gi 109150439 177 A 177
Cdd:COG3914  199 A 199
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
125-177 8.52e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 37.25  E-value: 8.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109150439 125 PSHYNYLQFAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYYTAMLGEEEA 177
Cdd:COG5010   88 PELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDE 140
 
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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