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Conserved domains on  [gi|1063724927|ref|NP_001329147|]
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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
6-230 5.12e-62

prolyl 4-hydroxylase; Provisional


The actual alignment was detected with superfamily member PLN00052:

Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 196.04  E-value: 5.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927   6 RVFLYRGFLSEEECDHLISLRKETTEvYSVDADGKT------------------QLDPVVAGIEEKVSAWTFLPGENGGS 67
Cdd:PLN00052   55 RIFVYKGFLSDAECDHLVKLAKKKIQ-RSMVADNKSgksvmsevrtssgmfldkRQDPVVSRIEERIAAWTFLPEENAEN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927  68 IKVRSYT-SEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNS---EMKPKN----SCLEGGNILRPVKG 139
Cdd:PLN00052  134 IQILRYEhGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwENQPKDdtfsECAHKGLAVKPVKG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927 140 NAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLI----YAKKQARIEESGECSDEDENCGRWAKLGECKKNPVYMIG 215
Cdd:PLN00052  214 DAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIhirsYEHPPVVPKDTEGCADKSAHCAEWAAAGECEKNPVYMVG 293
                         250
                  ....*....|....*
gi 1063724927 216 SPDYYGTCRKSCNAC 230
Cdd:PLN00052  294 AEGAPGNCRKSCGVC 308
 
Name Accession Description Interval E-value
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
6-230 5.12e-62

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 196.04  E-value: 5.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927   6 RVFLYRGFLSEEECDHLISLRKETTEvYSVDADGKT------------------QLDPVVAGIEEKVSAWTFLPGENGGS 67
Cdd:PLN00052   55 RIFVYKGFLSDAECDHLVKLAKKKIQ-RSMVADNKSgksvmsevrtssgmfldkRQDPVVSRIEERIAAWTFLPEENAEN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927  68 IKVRSYT-SEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNS---EMKPKN----SCLEGGNILRPVKG 139
Cdd:PLN00052  134 IQILRYEhGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwENQPKDdtfsECAHKGLAVKPVKG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927 140 NAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLI----YAKKQARIEESGECSDEDENCGRWAKLGECKKNPVYMIG 215
Cdd:PLN00052  214 DAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIhirsYEHPPVVPKDTEGCADKSAHCAEWAAAGECEKNPVYMVG 293
                         250
                  ....*....|....*
gi 1063724927 216 SPDYYGTCRKSCNAC 230
Cdd:PLN00052  294 AEGAPGNCRKSCGVC 308
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
98-176 1.40e-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: 1.40e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063724927   98 LATVVLYLSNTTQGGELLFPNSEMKPKNScleggniLRPVKGNAILFFtrllnaSLDGKSTHLRCPVVKGELLVATKLI 176
Cdd:smart00702  99 IATFILYLNDVEEGGELVFPGLRLMVVAT-------VKPKKGDLLFFP------SGHGRSLHGVCPVTRGSRWAITGWI 164
 
Name Accession Description Interval E-value
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
6-230 5.12e-62

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 196.04  E-value: 5.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927   6 RVFLYRGFLSEEECDHLISLRKETTEvYSVDADGKT------------------QLDPVVAGIEEKVSAWTFLPGENGGS 67
Cdd:PLN00052   55 RIFVYKGFLSDAECDHLVKLAKKKIQ-RSMVADNKSgksvmsevrtssgmfldkRQDPVVSRIEERIAAWTFLPEENAEN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927  68 IKVRSYT-SEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNS---EMKPKN----SCLEGGNILRPVKG 139
Cdd:PLN00052  134 IQILRYEhGQKYEPHFDYFHDKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwENQPKDdtfsECAHKGLAVKPVKG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724927 140 NAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLI----YAKKQARIEESGECSDEDENCGRWAKLGECKKNPVYMIG 215
Cdd:PLN00052  214 DAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIhirsYEHPPVVPKDTEGCADKSAHCAEWAAAGECEKNPVYMVG 293
                         250
                  ....*....|....*
gi 1063724927 216 SPDYYGTCRKSCNAC 230
Cdd:PLN00052  294 AEGAPGNCRKSCGVC 308
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
98-176 1.40e-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: 1.40e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063724927   98 LATVVLYLSNTTQGGELLFPNSEMKPKNScleggniLRPVKGNAILFFtrllnaSLDGKSTHLRCPVVKGELLVATKLI 176
Cdd:smart00702  99 IATFILYLNDVEEGGELVFPGLRLMVVAT-------VKPKKGDLLFFP------SGHGRSLHGVCPVTRGSRWAITGWI 164
ShKT smart00254
ShK toxin domain; ShK toxin domain
190-230 2.19e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 37.36  E-value: 2.19e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1063724927  190 CSDEDENCGRWAKlGECkKNPVYMigsPDYygtCRKSCNAC 230
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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