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Conserved domains on  [gi|30686940|ref|NP_194290|]
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Oxoglutarate/iron-dependent oxygenase [Arabidopsis thaliana]

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
 55-291 6.28e-66

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 208.37  E-value: 6.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940   55 DPTRVLQLSWLPRVFLYRGFLSEEECDHLISLRKETTEvYSVDADGKT------------------QLDPVVAGIEEKVS 116
Cdd:PLN00052  43 NASRVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQ-RSMVADNKSgksvmsevrtssgmfldkRQDPVVSRIEERIA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940  117 AWTFLPGENGGSIKVRSYT-SEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNS---EMKPKN----SC 188
Cdd:PLN00052 122 AWTFLPEENAENIQILRYEhGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwENQPKDdtfsEC 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940  189 LEGGNILRPVKGNAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLI----YAKKQARIEESGECSDEDENCGRWAKL 264
Cdd:PLN00052 202 AHKGLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIhirsYEHPPVVPKDTEGCADKSAHCAEWAAA 281

                        250       260
                 ....*....|....*....|....*..
gi 30686940  265 GECKKNPVYMIGSPDYYGTCRKSCNAC 291
Cdd:PLN00052 282 GECEKNPVYMVGAEGAPGNCRKSCGVC 308
 
Name Accession Description Interval E-value
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 55-291 6.28e-66

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 208.37  E-value: 6.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940   55 DPTRVLQLSWLPRVFLYRGFLSEEECDHLISLRKETTEvYSVDADGKT------------------QLDPVVAGIEEKVS 116
Cdd:PLN00052  43 NASRVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQ-RSMVADNKSgksvmsevrtssgmfldkRQDPVVSRIEERIA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940  117 AWTFLPGENGGSIKVRSYT-SEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNS---EMKPKN----SC 188
Cdd:PLN00052 122 AWTFLPEENAENIQILRYEhGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwENQPKDdtfsEC 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940  189 LEGGNILRPVKGNAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLI----YAKKQARIEESGECSDEDENCGRWAKL 264
Cdd:PLN00052 202 AHKGLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIhirsYEHPPVVPKDTEGCADKSAHCAEWAAA 281

                        250       260
                 ....*....|....*....|....*..
gi 30686940  265 GECKKNPVYMIGSPDYYGTCRKSCNAC 291
Cdd:PLN00052 282 GECEKNPVYMVGAEGAPGNCRKSCGVC 308
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 159-237 2.31e-07

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: 49.69  E-value: 2.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30686940    159 LATVVLYLSNTTQGGELLFPNSEMKPKNScleggniLRPVKGNAILFFtrllnaSLDGKSTHLRCPVVKGELLVATKLI 237
Cdd:smart00702  99 IATFILYLNDVEEGGELVFPGLRLMVVAT-------VKPKKGDLLFFP------SGHGRSLHGVCPVTRGSRWAITGWI 164
 
Name Accession Description Interval E-value
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 55-291 6.28e-66

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 208.37  E-value: 6.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940   55 DPTRVLQLSWLPRVFLYRGFLSEEECDHLISLRKETTEvYSVDADGKT------------------QLDPVVAGIEEKVS 116
Cdd:PLN00052  43 NASRVKAVSWQPRIFVYKGFLSDAECDHLVKLAKKKIQ-RSMVADNKSgksvmsevrtssgmfldkRQDPVVSRIEERIA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940  117 AWTFLPGENGGSIKVRSYT-SEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNS---EMKPKN----SC 188
Cdd:PLN00052 122 AWTFLPEENAENIQILRYEhGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwENQPKDdtfsEC 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686940  189 LEGGNILRPVKGNAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLI----YAKKQARIEESGECSDEDENCGRWAKL 264
Cdd:PLN00052 202 AHKGLAVKPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIhirsYEHPPVVPKDTEGCADKSAHCAEWAAA 281

                        250       260
                 ....*....|....*....|....*..
gi 30686940  265 GECKKNPVYMIGSPDYYGTCRKSCNAC 291
Cdd:PLN00052 282 GECEKNPVYMVGAEGAPGNCRKSCGVC 308
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 159-237 2.31e-07

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: 49.69  E-value: 2.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30686940    159 LATVVLYLSNTTQGGELLFPNSEMKPKNScleggniLRPVKGNAILFFtrllnaSLDGKSTHLRCPVVKGELLVATKLI 237
Cdd:smart00702  99 IATFILYLNDVEEGGELVFPGLRLMVVAT-------VKPKKGDLLFFP------SGHGRSLHGVCPVTRGSRWAITGWI 164
ShKT smart00254
ShK toxin domain; ShK toxin domain
 251-291 2.21e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 37.74  E-value: 2.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 30686940    251 CSDEDENCGRWAKlGECkKNPVYMigsPDYygtCRKSCNAC 291
Cdd:smart00254   1 CVDRHPDCAAWAK-GFC-TNPFYM---KSN---CPKTCGFC 33
 
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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