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Conserved domains on  [gi|446106020|ref|WP_000183875|]
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MULTISPECIES: 2OG-Fe(II) oxygenase [Bacillus]

Protein Classification

prolyl 4-hydroxylase family protein( domain architecture ID 707142)

prolyl 4-hydroxylase family protein belongs to the 2-oxoglutarate (2OG)-Fe(II) oxygenase superfamily, and may catalyze the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00052 super family cl28127
prolyl 4-hydroxylase; Provisional
38-215 8.45e-41

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 140.96  E-value: 8.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  38 EPLIVVLGNVISDEECNELIEMSKNKIKRSTIG---SARDV-NDIRTSSGAFLEENE--LTSKIEKRISSIMNVPVTHGE 111
Cdd:PLN00052  53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVAdnkSGKSVmSEVRTSSGMFLDKRQdpVVSRIEERIAAWTFLPEENAE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020 112 GLHILNYEVDQQYKAHYDYFAEHSRSA-ANNRISTLVMYLNDVEEGGETFFPKLN------------------LSVHPRK 172
Cdd:PLN00052 133 NIQILRYEHGQKYEPHFDYFHDKINQAlGGHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfsecahkgLAVKPVK 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446106020 173 GMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTY 215
Cdd:PLN00052 213 GDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSY 255
 
Name Accession Description Interval E-value
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
38-215 8.45e-41

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 140.96  E-value: 8.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  38 EPLIVVLGNVISDEECNELIEMSKNKIKRSTIG---SARDV-NDIRTSSGAFLEENE--LTSKIEKRISSIMNVPVTHGE 111
Cdd:PLN00052  53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVAdnkSGKSVmSEVRTSSGMFLDKRQdpVVSRIEERIAAWTFLPEENAE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020 112 GLHILNYEVDQQYKAHYDYFAEHSRSA-ANNRISTLVMYLNDVEEGGETFFPKLN------------------LSVHPRK 172
Cdd:PLN00052 133 NIQILRYEHGQKYEPHFDYFHDKINQAlGGHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfsecahkgLAVKPVK 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446106020 173 GMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTY 215
Cdd:PLN00052 213 GDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSY 255
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
49-211 9.16e-39

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: 131.36  E-value: 9.16e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020    49 SDEECNELIEMSKNKIKRST----IGSARDVNDIRTSSGAFL---EENELTSKIEKRISSIMNVP---VTHGEGLHILNY 118
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEvtrgIGNPNETSQYRQSNGTWLellERDLVIERIRQRLADFLGLLaglPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020   119 EVDQQYKAHYDYFAEhsrsaaNNRISTLVMYLNDVEEGGETFFPKLNLSVH----PRKGMAVYFEyfyqdqSLNELTLHG 194
Cdd:smart00702  81 GPGGHYGPHVDNFLY------GDRIATFILYLNDVEEGGELVFPGLRLMVVatvkPKKGDLLFFP------SGHGRSLHG 148
                          170
                   ....*....|....*..
gi 446106020   195 GAPVTKGEKWIATQWVR 211
Cdd:smart00702 149 VCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
113-211 4.24e-22

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: 86.28  E-value: 4.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  113 LHILNYEVDQQYKAHYDYFAEHSRSaaNNRISTLVMYLNDV--EEGGE-TFFPKLN-LSVHPRKGMAVYFEYfyqdqslN 188
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGG--GQRRLTVVLYLNDWeeEEGGElVLYDGDGvEDIKPKKGRLVLFPS-------S 71
                          90       100
                  ....*....|....*....|...
gi 446106020  189 ELTLHGGAPVTKGEKWIATQWVR 211
Cdd:pfam13640  72 ELSLHEVLPVTGGERWSITGWFR 94
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
31-179 4.45e-05

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: 42.62  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  31 QIISKFEEPLIVVLGNVISDEECNELIE-----MSKNKIKRSTIGSARD---VNDIRTSSGAFLEEnELTSKIEKRISSI 102
Cdd:COG3751    2 ALADALAAQGYVVIDDFLPPELAEALLAelpalDEAGAFKPAGIGRGLDhqvNEWIRRDSILWLDE-KLASAAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020 103 MN-----------VPVTHGEGlHILNYEVDQQYKAHYDYFaehsRSAANNRIStLVMYLNDV---EEGGE-----TFFPK 163
Cdd:COG3751   81 LEelrealnsplfLGLFEYEG-HFARYPPGGFYKRHLDAF----RGDLNRRLS-LVLYLNPDwqpEWGGElelydDDGSE 154
                        170
                 ....*....|....*.
gi 446106020 164 LNLSVHPRKGMAVYFE 179
Cdd:COG3751  155 EEVTVAPRFNRLVLFL 170
 
Name Accession Description Interval E-value
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
38-215 8.45e-41

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 140.96  E-value: 8.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  38 EPLIVVLGNVISDEECNELIEMSKNKIKRSTIG---SARDV-NDIRTSSGAFLEENE--LTSKIEKRISSIMNVPVTHGE 111
Cdd:PLN00052  53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVAdnkSGKSVmSEVRTSSGMFLDKRQdpVVSRIEERIAAWTFLPEENAE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020 112 GLHILNYEVDQQYKAHYDYFAEHSRSA-ANNRISTLVMYLNDVEEGGETFFPKLN------------------LSVHPRK 172
Cdd:PLN00052 133 NIQILRYEHGQKYEPHFDYFHDKINQAlGGHRYATVLMYLSTVDKGGETVFPNAEgwenqpkddtfsecahkgLAVKPVK 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446106020 173 GMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTY 215
Cdd:PLN00052 213 GDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSY 255
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
49-211 9.16e-39

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: 131.36  E-value: 9.16e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020    49 SDEECNELIEMSKNKIKRST----IGSARDVNDIRTSSGAFL---EENELTSKIEKRISSIMNVP---VTHGEGLHILNY 118
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEvtrgIGNPNETSQYRQSNGTWLellERDLVIERIRQRLADFLGLLaglPLSAEDAQVARY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020   119 EVDQQYKAHYDYFAEhsrsaaNNRISTLVMYLNDVEEGGETFFPKLNLSVH----PRKGMAVYFEyfyqdqSLNELTLHG 194
Cdd:smart00702  81 GPGGHYGPHVDNFLY------GDRIATFILYLNDVEEGGELVFPGLRLMVVatvkPKKGDLLFFP------SGHGRSLHG 148
                          170
                   ....*....|....*..
gi 446106020   195 GAPVTKGEKWIATQWVR 211
Cdd:smart00702 149 VCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
113-211 4.24e-22

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: 86.28  E-value: 4.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  113 LHILNYEVDQQYKAHYDYFAEHSRSaaNNRISTLVMYLNDV--EEGGE-TFFPKLN-LSVHPRKGMAVYFEYfyqdqslN 188
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAEGG--GQRRLTVVLYLNDWeeEEGGElVLYDGDGvEDIKPKKGRLVLFPS-------S 71
                          90       100
                  ....*....|....*....|...
gi 446106020  189 ELTLHGGAPVTKGEKWIATQWVR 211
Cdd:pfam13640  72 ELSLHEVLPVTGGERWSITGWFR 94
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
31-179 4.45e-05

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: 42.62  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020  31 QIISKFEEPLIVVLGNVISDEECNELIE-----MSKNKIKRSTIGSARD---VNDIRTSSGAFLEEnELTSKIEKRISSI 102
Cdd:COG3751    2 ALADALAAQGYVVIDDFLPPELAEALLAelpalDEAGAFKPAGIGRGLDhqvNEWIRRDSILWLDE-KLASAAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446106020 103 MN-----------VPVTHGEGlHILNYEVDQQYKAHYDYFaehsRSAANNRIStLVMYLNDV---EEGGE-----TFFPK 163
Cdd:COG3751   81 LEelrealnsplfLGLFEYEG-HFARYPPGGFYKRHLDAF----RGDLNRRLS-LVLYLNPDwqpEWGGElelydDDGSE 154
                        170
                 ....*....|....*.
gi 446106020 164 LNLSVHPRKGMAVYFE 179
Cdd:COG3751  155 EEVTVAPRFNRLVLFL 170
 
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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