NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|795477587|ref|XP_011892225|]
View 

PREDICTED: prolyl 3-hydroxylase 2 isoform X1 [Cercocebus atys]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
469-667 1.91e-32

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: 123.27  E-value: 1.91e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587   469 SEEQCRELHSVATGIMLVGDGYRGKTSP-HTPNEKFEGATVLKALKsgyegrvplksarlFYDISEKARRIVESYFMLns 547
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFLGL-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587   548 tlYFSYTHMVCRTALSGQQDrrnDLSHPIHADNCLldpeanecwkeppaYTFRDYSALLYMNDDFEGGEFIFTEMDAkTV 627
Cdd:smart00702  65 --LAGLPLSAEDAQVARYGP---GGHYGPHVDNFL--------------YGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 795477587   628 TASIKPKCGRMISFSSG-GENPHGVKAVTKGKRCAVALWFT 667
Cdd:smart00702 125 VATVKPKKGDLLFFPSGhGRSLHGVCPVTRGSRWAITGWIR 165
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
138-372 8.94e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.72  E-value: 8.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 138 VRSDFQRRVPYNYLQRAYIKLNQLEKAMEAAHTFFVANPEHMEMQQN-IENYRATA-GVEALQLVDREAKPHLES----Y 211
Cdd:COG2956   69 LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLlAEIYEQEGdWEKAIEVLERLLKLGPENahayC 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 212 NAGVKHYEADDFELAIRHFEQALREYfvediecrtlcegPQRFEEYEYLG---YKTGLYEAIADHYMQVLvcqhecvrel 288
Cdd:COG2956  149 ELAELYLEQGDYDEAIEALEKALKLD-------------PDCARALLLLAelyLEQGDYEEAIAALERAL---------- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 289 atrpgRLSPieNFLPLHYDyLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSidpasiEAREDLTMF 368
Cdd:COG2956  206 -----EQDP--DYLPALPR-LAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLE------AALALLERQ 271

                 ....
gi 795477587 369 VKRH 372
Cdd:COG2956  272 LRRH 275
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
469-667 1.91e-32

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: 123.27  E-value: 1.91e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587   469 SEEQCRELHSVATGIMLVGDGYRGKTSP-HTPNEKFEGATVLKALKsgyegrvplksarlFYDISEKARRIVESYFMLns 547
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFLGL-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587   548 tlYFSYTHMVCRTALSGQQDrrnDLSHPIHADNCLldpeanecwkeppaYTFRDYSALLYMNDDFEGGEFIFTEMDAkTV 627
Cdd:smart00702  65 --LAGLPLSAEDAQVARYGP---GGHYGPHVDNFL--------------YGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 795477587   628 TASIKPKCGRMISFSSG-GENPHGVKAVTKGKRCAVALWFT 667
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 ...
576-666 4.55e-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: 65.48  E-value: 4.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587  576 IHADNCLLDPEANEcwkeppaytfRDYSALLYMND--DFEGGEFIFTEMDAktvTASIKPKCGRMISFSSGGENPHGVKA 653
Cdd:pfam13640  14 PHLDFFEGAEGGGQ----------RRLTVVLYLNDweEEEGGELVLYDGDG---VEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 795477587  654 VTKGKRCAVALWF 666
Cdd:pfam13640  81 VTGGERWSITGWF 93
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
600-666 1.41e-07

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 52.25  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 600 RDYSALLYMNDD---FEGGEFIFTEMDAKTVTASIKPKCGRMISFSSgGENPHGVKAVtKGKRCAVALWF 666
Cdd:COG3751  125 RRLSLVLYLNPDwqpEWGGELELYDDDGSEEEVTVAPRFNRLVLFLS-EEFPHEVLPV-GRERLSIAGWF 192
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
138-372 8.94e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.72  E-value: 8.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 138 VRSDFQRRVPYNYLQRAYIKLNQLEKAMEAAHTFFVANPEHMEMQQN-IENYRATA-GVEALQLVDREAKPHLES----Y 211
Cdd:COG2956   69 LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLlAEIYEQEGdWEKAIEVLERLLKLGPENahayC 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 212 NAGVKHYEADDFELAIRHFEQALREYfvediecrtlcegPQRFEEYEYLG---YKTGLYEAIADHYMQVLvcqhecvrel 288
Cdd:COG2956  149 ELAELYLEQGDYDEAIEALEKALKLD-------------PDCARALLLLAelyLEQGDYEEAIAALERAL---------- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 289 atrpgRLSPieNFLPLHYDyLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSidpasiEAREDLTMF 368
Cdd:COG2956  206 -----EQDP--DYLPALPR-LAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLE------AALALLERQ 271

                 ....
gi 795477587 369 VKRH 372
Cdd:COG2956  272 LRRH 275
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
469-667 1.91e-32

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: 123.27  E-value: 1.91e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587   469 SEEQCRELHSVATGIMLVGDGYRGKTSP-HTPNEKFEGATVLKALKsgyegrvplksarlFYDISEKARRIVESYFMLns 547
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPnETSQYRQSNGTWLELLE--------------RDLVIERIRQRLADFLGL-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587   548 tlYFSYTHMVCRTALSGQQDrrnDLSHPIHADNCLldpeanecwkeppaYTFRDYSALLYMNDDFEGGEFIFTEMDAkTV 627
Cdd:smart00702  65 --LAGLPLSAEDAQVARYGP---GGHYGPHVDNFL--------------YGDRIATFILYLNDVEEGGELVFPGLRL-MV 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 795477587   628 TASIKPKCGRMISFSSG-GENPHGVKAVTKGKRCAVALWFT 667
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 ...
576-666 4.55e-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: 65.48  E-value: 4.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587  576 IHADNCLLDPEANEcwkeppaytfRDYSALLYMND--DFEGGEFIFTEMDAktvTASIKPKCGRMISFSSGGENPHGVKA 653
Cdd:pfam13640  14 PHLDFFEGAEGGGQ----------RRLTVVLYLNDweEEEGGELVLYDGDG---VEDIKPKKGRLVLFPSSELSLHEVLP 80
                          90
                  ....*....|...
gi 795477587  654 VTKGKRCAVALWF 666
Cdd:pfam13640  81 VTGGERWSITGWF 93
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
600-666 1.41e-07

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 52.25  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 600 RDYSALLYMNDD---FEGGEFIFTEMDAKTVTASIKPKCGRMISFSSgGENPHGVKAVtKGKRCAVALWF 666
Cdd:COG3751  125 RRLSLVLYLNPDwqpEWGGELELYDDDGSEEEVTVAPRFNRLVLFLS-EEFPHEVLPV-GRERLSIAGWF 192
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
138-372 8.94e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.72  E-value: 8.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 138 VRSDFQRRVPYNYLQRAYIKLNQLEKAMEAAHTFFVANPEHMEMQQN-IENYRATA-GVEALQLVDREAKPHLES----Y 211
Cdd:COG2956   69 LERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLlAEIYEQEGdWEKAIEVLERLLKLGPENahayC 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 212 NAGVKHYEADDFELAIRHFEQALREYfvediecrtlcegPQRFEEYEYLG---YKTGLYEAIADHYMQVLvcqhecvrel 288
Cdd:COG2956  149 ELAELYLEQGDYDEAIEALEKALKLD-------------PDCARALLLLAelyLEQGDYEEAIAALERAL---------- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 289 atrpgRLSPieNFLPLHYDyLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSidpasiEAREDLTMF 368
Cdd:COG2956  206 -----EQDP--DYLPALPR-LAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLE------AALALLERQ 271

                 ....
gi 795477587 369 VKRH 372
Cdd:COG2956  272 LRRH 275
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
44-235 1.02e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 45.75  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587  44 DLLYASGAAAYYSGDYRQAVRDLEAALRSHRRLREIRTRcARHCAARHPLAPLGEGPGAELPLFRSLLGRARCYRSCETQ 123
Cdd:COG3914   11 ALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLA-ALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 124 RLGgpasRHRVSEDVRSDFQRRVP-----YNYLQRAYIKLNQLEKAMEAAHTFFVANPEHMEMQQNI-----ENYRATAG 193
Cdd:COG3914   90 ALG----RYEEALALYRRALALNPdnaeaLFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLgealrRLGRLEEA 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 795477587 194 VEALQLVDREAKPHLESYNA-GVKHYEADDFELAIRHFEQALR 235
Cdd:COG3914  166 IAALRRALELDPDNAEALNNlGNALQDLGRLEEAIAAYRRALE 208
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
143-342 8.60e-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: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 143 QRRVPYNYLQRAYIKLNQLEKAMEAAHTFFVANPEHMEMQQNIENYRATAGVEALQLVDREAKPHLESYNAGVKHYEADD 222
Cdd:COG3914   14 AAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477587 223 FELAIRHFEQALREYfvediecrtlcegPQRFEEYEYLG---YKTGLYEAIADHYMQVLvcqhecvrelatrpgRLSPie 299
Cdd:COG3914   94 YEEALALYRRALALN-------------PDNAEALFNLGnllLALGRLEEALAALRRAL---------------ALNP-- 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 795477587 300 NFLPLHYDYLQfAYYRVGEYVKALECAKAYLLCHPDDEDVLDN 342
Cdd:COG3914  144 DFAEAYLNLGE-ALRRLGRLEEAIAALRRALELDPDNAEALNN 185
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH