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Conserved domains on  [gi|109150433|ref|NP_062757|]
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prolyl 3-hydroxylase 1 isoform 2 precursor [Mus musculus]

Protein Classification

2OG-Fe(II) oxygenase( domain architecture ID 13540654)

2OG-Fe(II) oxygenase belonging to the large and diverse Fe(II)- and 2-oxoglutarate (2-OG)-dependent dioxygenase superfamily that share a common reaction mechanism, using Fe(II) and the cosubstrate 2-OG in the active site to activate oxygen, resulting in the two-electron oxidation of the target substrate

CATH:  2.60.120.620
EC:  1.14.11.-
Gene Ontology:  GO:0008198|GO:0016705

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 ...
482-680 1.49e-35

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: 132.13  E-value: 1.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   482 SDDECQELQRLTNAAATSGDGYRGQTSP-HTPNEKFYGVTVLKALKlgqegkvplqsarmYYNVTEKVRRVMESYFrldt 560
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   561 PLYFSYSHLVCRTAIEESQaerKDSSHPVHVDNCilnaealmcikeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 640
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 109150433   641 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 680
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
PEP_TPR_lipo super family cl37187
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
90-337 7.98e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


The actual alignment was detected with superfamily member TIGR02917:

Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 49.31  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   90 LDLGPDPSLSQDPGAAALHDLRffgavlrraaclrrclgpPSAHLLSEELD---------LEFNKRSPYNYLQVAYFKI- 159
Cdd:TIGR02917 110 LDELPGKTLLDDEGAAELLALR------------------GLAYLGLGQLElaqksyeqaLAIDPRSLYAKLGLAQLALa 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  160 -NKLEKAVAAAHTFFVGNPEHME---MRQNLDYYQTMSGVKEADFRD-LEAKPH--MHEFRLGVRLYSEEKPQEAVPHLE 232
Cdd:TIGR02917 172 eNRFDEARALIDEVLTADPGNVDallLKGDLLLSLGNIELALAAYRKaIALRPNniAVLLALATILIEAGEFEEAEKHAD 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  233 AALQ--------EYFvadeecRALcegpydydgynyLDYSADLFQAITDHYVQVLncKQNcvtelashpsrekpfedflP 304
Cdd:TIGR02917 252 ALLKkapnsplaHYL------KAL------------VDFQKKNYEDARETLQDAL--KSA-------------------P 292
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 109150433  305 SHYNYLQFA---YYNIGNYTQAIECAKTYLLFFPND 337
Cdd:TIGR02917 293 EYLPALLLAgasEYQLGNLEQAYQYLNQILKYAPNS 328
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
482-680 1.49e-35

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: 132.13  E-value: 1.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   482 SDDECQELQRLTNAAATSGDGYRGQTSP-HTPNEKFYGVTVLKALKlgqegkvplqsarmYYNVTEKVRRVMESYFrldt 560
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   561 PLYFSYSHLVCRTAIEESQaerKDSSHPVHVDNCilnaealmcikeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 640
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 109150433   641 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 680
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 ...
589-679 2.30e-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: 63.55  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  589 VHVDNCILNAEALmcikeppaytFRDYSAILYLNG--DFDGGNFyftELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKA 666
Cdd:pfam13640  14 PHLDFFEGAEGGG----------QRRLTVVLYLNDweEEEGGEL---VLYDGDGVEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 109150433  667 VTRGQRCAIALWF 679
Cdd:pfam13640  81 VTGGERWSITGWF 93
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
90-337 7.98e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 49.31  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   90 LDLGPDPSLSQDPGAAALHDLRffgavlrraaclrrclgpPSAHLLSEELD---------LEFNKRSPYNYLQVAYFKI- 159
Cdd:TIGR02917 110 LDELPGKTLLDDEGAAELLALR------------------GLAYLGLGQLElaqksyeqaLAIDPRSLYAKLGLAQLALa 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  160 -NKLEKAVAAAHTFFVGNPEHME---MRQNLDYYQTMSGVKEADFRD-LEAKPH--MHEFRLGVRLYSEEKPQEAVPHLE 232
Cdd:TIGR02917 172 eNRFDEARALIDEVLTADPGNVDallLKGDLLLSLGNIELALAAYRKaIALRPNniAVLLALATILIEAGEFEEAEKHAD 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  233 AALQ--------EYFvadeecRALcegpydydgynyLDYSADLFQAITDHYVQVLncKQNcvtelashpsrekpfedflP 304
Cdd:TIGR02917 252 ALLKkapnsplaHYL------KAL------------VDFQKKNYEDARETLQDAL--KSA-------------------P 292
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 109150433  305 SHYNYLQFA---YYNIGNYTQAIECAKTYLLFFPND 337
Cdd:TIGR02917 293 EYLPALLLAgasEYQLGNLEQAYQYLNQILKYAPNS 328
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
117-356 5.37e-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: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 117 LRRAACLRRCLGPPSAHLLSEELDLEFNKRSPYNYLQVAYFKINKLEKAVAAAhtffvgnpehmemrqnldyYQTMSGVK 196
Cdd:COG3914    6 LLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAA-------------------LLALAAGE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 197 EADFRDLEAKPHMHEFRLGVRLYSEEKPQEAVPHLEAALQEYfvadeecralcegPYDYDGYNYLdysADLFQAItDHYV 276
Cdd:COG3914   67 AAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN-------------PDNAEALFNL---GNLLLAL-GRLE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 277 QVLNCKQNCvteLASHPsrekpfeDFLPSHYNYLQfAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYYTAMLGE-EE 355
Cdd:COG3914  130 EALAALRRA---LALNP-------DFAEAYLNLGE-ALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRlEE 198

                 .
gi 109150433 356 A 356
Cdd:COG3914  199 A 199
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
482-680 1.49e-35

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: 132.13  E-value: 1.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   482 SDDECQELQRLTNAAATSGDGYRGQTSP-HTPNEKFYGVTVLKALKlgqegkvplqsarmYYNVTEKVRRVMESYFrldt 560
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFL---- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   561 PLYFSYSHLVCRTAIEESQaerKDSSHPVHVDNCilnaealmcikeppAYTFRDYSAILYLNGDFDGGNFYFTELDAkTV 640
Cdd:smart00702  63 GLLAGLPLSAEDAQVARYG---PGGHYGPHVDNF--------------LYGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 109150433   641 TAEVQPQCGRAVGFSSG-TENPHGVKAVTRGQRCAIALWFT 680
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 ...
589-679 2.30e-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: 63.55  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  589 VHVDNCILNAEALmcikeppaytFRDYSAILYLNG--DFDGGNFyftELDAKTVTAEVQPQCGRAVGFSSGTENPHGVKA 666
Cdd:pfam13640  14 PHLDFFEGAEGGG----------QRRLTVVLYLNDweEEEGGEL---VLYDGDGVEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 109150433  667 VTRGQRCAIALWF 679
Cdd:pfam13640  81 VTGGERWSITGWF 93
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
90-337 7.98e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 49.31  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433   90 LDLGPDPSLSQDPGAAALHDLRffgavlrraaclrrclgpPSAHLLSEELD---------LEFNKRSPYNYLQVAYFKI- 159
Cdd:TIGR02917 110 LDELPGKTLLDDEGAAELLALR------------------GLAYLGLGQLElaqksyeqaLAIDPRSLYAKLGLAQLALa 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  160 -NKLEKAVAAAHTFFVGNPEHME---MRQNLDYYQTMSGVKEADFRD-LEAKPH--MHEFRLGVRLYSEEKPQEAVPHLE 232
Cdd:TIGR02917 172 eNRFDEARALIDEVLTADPGNVDallLKGDLLLSLGNIELALAAYRKaIALRPNniAVLLALATILIEAGEFEEAEKHAD 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433  233 AALQ--------EYFvadeecRALcegpydydgynyLDYSADLFQAITDHYVQVLncKQNcvtelashpsrekpfedflP 304
Cdd:TIGR02917 252 ALLKkapnsplaHYL------KAL------------VDFQKKNYEDARETLQDAL--KSA-------------------P 292
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 109150433  305 SHYNYLQFA---YYNIGNYTQAIECAKTYLLFFPND 337
Cdd:TIGR02917 293 EYLPALLLAgasEYQLGNLEQAYQYLNQILKYAPNS 328
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
117-356 5.37e-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: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 117 LRRAACLRRCLGPPSAHLLSEELDLEFNKRSPYNYLQVAYFKINKLEKAVAAAhtffvgnpehmemrqnldyYQTMSGVK 196
Cdd:COG3914    6 LLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAA-------------------LLALAAGE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 197 EADFRDLEAKPHMHEFRLGVRLYSEEKPQEAVPHLEAALQEYfvadeecralcegPYDYDGYNYLdysADLFQAItDHYV 276
Cdd:COG3914   67 AAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN-------------PDNAEALFNL---GNLLLAL-GRLE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 277 QVLNCKQNCvteLASHPsrekpfeDFLPSHYNYLQfAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYYTAMLGE-EE 355
Cdd:COG3914  130 EALAALRRA---LALNP-------DFAEAYLNLGE-ALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRlEE 198

                 .
gi 109150433 356 A 356
Cdd:COG3914  199 A 199
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
203-383 7.49e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 203 LEAKPHMHE--FRLGVRLYSEEKPQEAVPHLEAALQEyfvadeecralceGPYDYDGYNYLD---YSADLFQAITDHYVQ 277
Cdd:COG3914  105 LALNPDNAEalFNLGNLLLALGRLEEALAALRRALAL-------------NPDFAEAYLNLGealRRLGRLEEAIAALRR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150433 278 VLnckqncvtelashpsREKPfeDFLPSHYNyLQFAYYNIGNYTQAIECAKTYLLFFPNDEVMHQNLAYytAMLGEEEAS 357
Cdd:COG3914  172 AL---------------ELDP--DNAEALNN-LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLF--ALRQACDWE 231
                        170       180
                 ....*....|....*....|....*.
gi 109150433 358 SISPRENAEEYRRRSLLEKELLFFAY 383
Cdd:COG3914  232 VYDRFEELLAALARGPSELSPFALLY 257
 
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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