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Conserved domains on  [gi|489050593|ref|WP_002960803|]
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MULTISPECIES: Fe2+-dependent dioxygenase [Pseudoalteromonas]

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 ...
2-226 1.99e-161

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


:

Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 444.97  E-value: 1.99e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   2 IVKIPELLTKEEVAYCHEVLLKAQWADGSITAGHQSTKAKNNLQLPENSPECQELGDIIMAALARSNLFMSAALPAKIFP 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593  82 PLFNCYQGGQSFGVHVDNAIRQVPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPSTSLHRV 161
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGQRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489050593 162 MPVTSGRRLASFFWLQSMVNSDEKRGLLFDLDMSIQSLRSKVEDSPEIIQLTGVYHNLLRQWAQT 226
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 ...
2-226 1.99e-161

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


Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 444.97  E-value: 1.99e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   2 IVKIPELLTKEEVAYCHEVLLKAQWADGSITAGHQSTKAKNNLQLPENSPECQELGDIIMAALARSNLFMSAALPAKIFP 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593  82 PLFNCYQGGQSFGVHVDNAIRQVPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPSTSLHRV 161
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGQRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489050593 162 MPVTSGRRLASFFWLQSMVNSDEKRGLLFDLDMSIQSLRSKVEDSPEIIQLTGVYHNLLRQWAQT 226
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
PRK05467 PRK05467
Fe(II)-dependent oxygenase superfamily protein; Provisional
1-226 6.27e-155

Fe(II)-dependent oxygenase superfamily protein; Provisional


Pssm-ID: 235483 [Multi-domain]  Cd Length: 226  Bit Score: 428.48  E-value: 6.27e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   1 MIVKIPELLTKEEVAYCHEVLLKAQWADGSITAGHQSTKAKNNLQLPENSPECQELGDIIMAALARSNLFMSAALPAKIF 80
Cdd:PRK05467   1 MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLFFSAALPRKIH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593  81 PPLFNCYQGGQSFGVHVDNAIRQVPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPSTSLHR 160
Cdd:PRK05467  81 PPLFNRYEGGMSYGFHVDNAVRSLPGTGGRVRTDLSATLFLSDPDDYDGGELVIEDTYGEHRVKLPAGDLVLYPSTSLHR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489050593 161 VMPVTSGRRLASFFWLQSMVNSDEKRGLLFDLDMSIQSLRSKVEDSPEIIQLTGVYHNLLRQWAQT 226
Cdd:PRK05467 161 VTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELDLLTGVYHNLLRRWAEV 226
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
10-177 6.68e-26

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: 98.61  E-value: 6.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593    10 TKEEVAYCHEVLLKAQWADG---SITAGHQSTKAKNNLQLPENSPECQELGDIIMAaLARSNLFMSAALPAKIFPPLFNC 86
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEvtrGIGNPNETSQYRQSNGTWLELLERDLVIERIRQ-RLADFLGLLAGLPLSAEDAQVAR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593    87 YQGGQSFGVHVDNairqvpgtPVKIRTDVSMTLFINDPEdyEGGELVIEDTYGS--HSVKLPAGSMVLYPS---TSLHRV 161
Cdd:smart00702  80 YGPGGHYGPHVDN--------FLYGDRIATFILYLNDVE--EGGELVFPGLRLMvvATVKPKKGDLLFFPSghgRSLHGV 149
                          170
                   ....*....|....*.
gi 489050593   162 MPVTSGRRLASFFWLQ 177
Cdd:smart00702 150 CPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
84-176 7.20e-24

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: 91.28  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   84 FNCYQGGQSFGVHVDNAirqvPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPST--SLHRV 161
Cdd:pfam13640   3 LARYGDGGFYKPHLDFF----EGAEGGGQRRLTVVLYLNDWEEEEGGELVLYDGDGVEDIKPKKGRLVLFPSSelSLHEV 78
                          90
                  ....*....|....*
gi 489050593  162 MPVTSGRRLASFFWL 176
Cdd:pfam13640  79 LPVTGGERWSITGWF 93
 
Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-226 1.99e-161

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


Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 444.97  E-value: 1.99e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   2 IVKIPELLTKEEVAYCHEVLLKAQWADGSITAGHQSTKAKNNLQLPENSPECQELGDIIMAALARSNLFMSAALPAKIFP 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593  82 PLFNCYQGGQSFGVHVDNAIRQVPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPSTSLHRV 161
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGQRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489050593 162 MPVTSGRRLASFFWLQSMVNSDEKRGLLFDLDMSIQSLRSKVEDSPEIIQLTGVYHNLLRQWAQT 226
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
PRK05467 PRK05467
Fe(II)-dependent oxygenase superfamily protein; Provisional
1-226 6.27e-155

Fe(II)-dependent oxygenase superfamily protein; Provisional


Pssm-ID: 235483 [Multi-domain]  Cd Length: 226  Bit Score: 428.48  E-value: 6.27e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   1 MIVKIPELLTKEEVAYCHEVLLKAQWADGSITAGHQSTKAKNNLQLPENSPECQELGDIIMAALARSNLFMSAALPAKIF 80
Cdd:PRK05467   1 MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLFFSAALPRKIH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593  81 PPLFNCYQGGQSFGVHVDNAIRQVPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPSTSLHR 160
Cdd:PRK05467  81 PPLFNRYEGGMSYGFHVDNAVRSLPGTGGRVRTDLSATLFLSDPDDYDGGELVIEDTYGEHRVKLPAGDLVLYPSTSLHR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489050593 161 VMPVTSGRRLASFFWLQSMVNSDEKRGLLFDLDMSIQSLRSKVEDSPEIIQLTGVYHNLLRQWAQT 226
Cdd:PRK05467 161 VTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELDLLTGVYHNLLRRWAEV 226
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
10-177 6.68e-26

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: 98.61  E-value: 6.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593    10 TKEEVAYCHEVLLKAQWADG---SITAGHQSTKAKNNLQLPENSPECQELGDIIMAaLARSNLFMSAALPAKIFPPLFNC 86
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEvtrGIGNPNETSQYRQSNGTWLELLERDLVIERIRQ-RLADFLGLLAGLPLSAEDAQVAR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593    87 YQGGQSFGVHVDNairqvpgtPVKIRTDVSMTLFINDPEdyEGGELVIEDTYGS--HSVKLPAGSMVLYPS---TSLHRV 161
Cdd:smart00702  80 YGPGGHYGPHVDN--------FLYGDRIATFILYLNDVE--EGGELVFPGLRLMvvATVKPKKGDLLFFPSghgRSLHGV 149
                          170
                   ....*....|....*.
gi 489050593   162 MPVTSGRRLASFFWLQ 177
Cdd:smart00702 150 CPVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
84-176 7.20e-24

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: 91.28  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593   84 FNCYQGGQSFGVHVDNAirqvPGTPVKIRTDVSMTLFINDPEDYEGGELVIEDTYGSHSVKLPAGSMVLYPST--SLHRV 161
Cdd:pfam13640   3 LARYGDGGFYKPHLDFF----EGAEGGGQRRLTVVLYLNDWEEEEGGELVLYDGDGVEDIKPKKGRLVLFPSSelSLHEV 78
                          90
                  ....*....|....*
gi 489050593  162 MPVTSGRRLASFFWL 176
Cdd:pfam13640  79 LPVTGGERWSITGWF 93
PKHD_C pfam18331
PKHD-type hydroxylase C-terminal domain; This is the C-terminal domain found in PKHD-type ...
183-224 1.12e-22

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: 86.37  E-value: 1.12e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 489050593  183 DEKRGLLFDLDMSIQSLRSKVEDSPEIIQLTGVYHNLLRQWA 224
Cdd:pfam18331   1 DAQRRLLFDLDQAIQRLRADLGDDPAVVGLTGVYHNLLRRWA 42
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
86-175 3.66e-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: 43.01  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489050593  86 CYQGGQSFGVHVDNairqvpGTPVKIRTdVSMTLFIND---PEDyeGGELVIEDTYGSHSVK--LP-AGSMVLYPSTSL- 158
Cdd:COG3751  105 RYPPGGFYKRHLDA------FRGDLNRR-LSLVLYLNPdwqPEW--GGELELYDDDGSEEEVtvAPrFNRLVLFLSEEFp 175
                         90
                 ....*....|....*...
gi 489050593 159 HRVMPVTSGRR-LASFFW 175
Cdd:COG3751  176 HEVLPVGRERLsIAGWFR 193
 
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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