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Conserved domains on  [gi|739563987|ref|WP_037422119|]
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MULTISPECIES: Fe2+-dependent dioxygenase [Shewanella]

Protein Classification

PKHD-type hydroxylase( domain architecture ID 10006949)

PKHD-type hydroxylase similar to Escherichia coli YbiX, which belongs to a family of 2-oxoglutarate and Fe(II)-dependent oxygenases that catalyze reactions such as oxidation of an organic substrate using a dioxygen molecule

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-224 1.57e-142

Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only];


:

Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 397.21  E-value: 1.57e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   2 LIEIPHVFSKQEVNQLREQLDARTWIDGNQTSGVMASTRKRNQQLDKDDPVAIGIGELIMERLLAHPLFVSAALPLQFYP 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987  82 PLFNRYQGGETFGYHIDNAIRSTSDGM--VRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPSTSLHQV 159
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGqrVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739563987 160 TPVTSGERTAAFMWLQSMVRDEGQRRLLFQLDQSIQSLTSQTAPEQELFNLTGVYHNLLRRWSEL 224
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
 
Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-224 1.57e-142

Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only];


Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 397.21  E-value: 1.57e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   2 LIEIPHVFSKQEVNQLREQLDARTWIDGNQTSGVMASTRKRNQQLDKDDPVAIGIGELIMERLLAHPLFVSAALPLQFYP 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987  82 PLFNRYQGGETFGYHIDNAIRSTSDGM--VRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPSTSLHQV 159
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGqrVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739563987 160 TPVTSGERTAAFMWLQSMVRDEGQRRLLFQLDQSIQSLTSQTAPEQELFNLTGVYHNLLRRWSEL 224
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
PRK05467 PRK05467
Fe(II)-dependent oxygenase superfamily protein; Provisional
1-224 4.29e-141

Fe(II)-dependent oxygenase superfamily protein; Provisional


Pssm-ID: 235483 [Multi-domain]  Cd Length: 226  Bit Score: 393.42  E-value: 4.29e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   1 MLIEIPHVFSKQEVNQLREQLDARTWIDGNQTSGVMASTRKRNQQLDKDDPVAIGIGELIMERLLAHPLFVSAALPLQFY 80
Cdd:PRK05467   1 MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLFFSAALPRKIH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987  81 PPLFNRYQGGETFGYHIDNAIRST--SDGMVRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPSTSLHQ 158
Cdd:PRK05467  81 PPLFNRYEGGMSYGFHVDNAVRSLpgTGGRVRTDLSATLFLSDPDDYDGGELVIEDTYGEHRVKLPAGDLVLYPSTSLHR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739563987 159 VTPVTSGERTAAFMWLQSMVRDEGQRRLLFQLDQSIQSLTSQTAPEQELFNLTGVYHNLLRRWSEL 224
Cdd:PRK05467 161 VTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELDLLTGVYHNLLRRWAEV 226
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
10-175 1.55e-24

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: 95.15  E-value: 1.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987    10 SKQEVNQLREQLDARTW----IDGNQTSGVMASTRKRNQ---QLDKDDPVAigigELIMERLLAHpLFVSAALPLQFYPP 82
Cdd:smart00702   1 SPAECQKLLEEAEPLGWrgevTRGIGNPNETSQYRQSNGtwlELLERDLVI----ERIRQRLADF-LGLLAGLPLSAEDA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987    83 LFNRYQGGETFGYHIDNAIRSTSDgmvrtdLSATLFLSEPdtYQGGELVIQDTYGQ--QSIKLAAGSLVLYPS---TSLH 157
Cdd:smart00702  76 QVARYGPGGHYGPHVDNFLYGDRI------ATFILYLNDV--EEGGELVFPGLRLMvvATVKPKKGDLLFFPSghgRSLH 147
                          170
                   ....*....|....*...
gi 739563987   158 QVTPVTSGERTAAFMWLQ 175
Cdd:smart00702 148 GVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
84-174 1.56e-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: 87.43  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   84 FNRYQGGETFGYHIDNAIRSTSDGmvRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPST--SLHQVTP 161
Cdd:pfam13640   3 LARYGDGGFYKPHLDFFEGAEGGG--QRRLTVVLYLNDWEEEEGGELVLYDGDGVEDIKPKKGRLVLFPSSelSLHEVLP 80
                          90
                  ....*....|...
gi 739563987  162 VTSGERTAAFMWL 174
Cdd:pfam13640  81 VTGGERWSITGWF 93
 
Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-224 1.57e-142

Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only];


Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 397.21  E-value: 1.57e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   2 LIEIPHVFSKQEVNQLREQLDARTWIDGNQTSGVMASTRKRNQQLDKDDPVAIGIGELIMERLLAHPLFVSAALPLQFYP 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987  82 PLFNRYQGGETFGYHIDNAIRSTSDGM--VRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPSTSLHQV 159
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGqrVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739563987 160 TPVTSGERTAAFMWLQSMVRDEGQRRLLFQLDQSIQSLTSQTAPEQELFNLTGVYHNLLRRWSEL 224
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
PRK05467 PRK05467
Fe(II)-dependent oxygenase superfamily protein; Provisional
1-224 4.29e-141

Fe(II)-dependent oxygenase superfamily protein; Provisional


Pssm-ID: 235483 [Multi-domain]  Cd Length: 226  Bit Score: 393.42  E-value: 4.29e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   1 MLIEIPHVFSKQEVNQLREQLDARTWIDGNQTSGVMASTRKRNQQLDKDDPVAIGIGELIMERLLAHPLFVSAALPLQFY 80
Cdd:PRK05467   1 MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLFFSAALPRKIH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987  81 PPLFNRYQGGETFGYHIDNAIRST--SDGMVRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPSTSLHQ 158
Cdd:PRK05467  81 PPLFNRYEGGMSYGFHVDNAVRSLpgTGGRVRTDLSATLFLSDPDDYDGGELVIEDTYGEHRVKLPAGDLVLYPSTSLHR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739563987 159 VTPVTSGERTAAFMWLQSMVRDEGQRRLLFQLDQSIQSLTSQTAPEQELFNLTGVYHNLLRRWSEL 224
Cdd:PRK05467 161 VTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELDLLTGVYHNLLRRWAEV 226
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
10-175 1.55e-24

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: 95.15  E-value: 1.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987    10 SKQEVNQLREQLDARTW----IDGNQTSGVMASTRKRNQ---QLDKDDPVAigigELIMERLLAHpLFVSAALPLQFYPP 82
Cdd:smart00702   1 SPAECQKLLEEAEPLGWrgevTRGIGNPNETSQYRQSNGtwlELLERDLVI----ERIRQRLADF-LGLLAGLPLSAEDA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987    83 LFNRYQGGETFGYHIDNAIRSTSDgmvrtdLSATLFLSEPdtYQGGELVIQDTYGQ--QSIKLAAGSLVLYPS---TSLH 157
Cdd:smart00702  76 QVARYGPGGHYGPHVDNFLYGDRI------ATFILYLNDV--EEGGELVFPGLRLMvvATVKPKKGDLLFFPSghgRSLH 147
                          170
                   ....*....|....*...
gi 739563987   158 QVTPVTSGERTAAFMWLQ 175
Cdd:smart00702 148 GVCPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
84-174 1.56e-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: 87.43  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   84 FNRYQGGETFGYHIDNAIRSTSDGmvRTDLSATLFLSEPDTYQGGELVIQDTYGQQSIKLAAGSLVLYPST--SLHQVTP 161
Cdd:pfam13640   3 LARYGDGGFYKPHLDFFEGAEGGG--QRRLTVVLYLNDWEEEEGGELVLYDGDGVEDIKPKKGRLVLFPSSelSLHEVLP 80
                          90
                  ....*....|...
gi 739563987  162 VTSGERTAAFMWL 174
Cdd:pfam13640  81 VTGGERWSITGWF 93
PKHD_C pfam18331
PKHD-type hydroxylase C-terminal domain; This is the C-terminal domain found in PKHD-type ...
182-223 2.00e-16

PKHD-type hydroxylase C-terminal domain; This is the C-terminal domain found in PKHD-type hydroxylase enzymes. Family members are found mostly in Bacteria and carry the 2OG-Fe(II) oxygenase superfamily pfam13640.


Pssm-ID: 436417 [Multi-domain]  Cd Length: 43  Bit Score: 70.19  E-value: 2.00e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 739563987  182 GQRRLLFQLDQSIQSLTSQTAPEQELFNLTGVYHNLLRRWSE 223
Cdd:pfam18331   2 AQRRLLFDLDQAIQRLRADLGDDPAVVGLTGVYHNLLRRWAE 43
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
5-162 1.61e-03

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: 38.00  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987   5 IPHVFSKQEVNQLREQLDARTWIDGNQTSGVmasTRKRNQQLDKD--------------DPVAIGIGElIMERLLAH--- 67
Cdd:COG3751   15 IDDFLPPELAEALLAELPALDEAGAFKPAGI---GRGLDHQVNEWirrdsilwldeklaSAAQARYLA-ALEELREAlns 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739563987  68 PLFvsaaLPLQFYPPLFNRYQGGETFGYHIDNAiRSTSDgmvRTdLSATLFLSE-PDTYQGGELVIQDTYGQQSIKL--- 143
Cdd:COG3751   91 PLF----LGLFEYEGHFARYPPGGFYKRHLDAF-RGDLN---RR-LSLVLYLNPdWQPEWGGELELYDDDGSEEEVTvap 161
                        170       180
                 ....*....|....*....|
gi 739563987 144 AAGSLVLYPSTSL-HQVTPV 162
Cdd:COG3751  162 RFNRLVLFLSEEFpHEVLPV 181
 
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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