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Conserved domains on  [gi|1017483972|ref|NP_001309681|]
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JmjC domain-containing protein [Caenorhabditis elegans]

Protein Classification

bifunctional arginine demethylase and lysyl-hydroxylase( domain architecture ID 10492996)

bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 is a dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 73-180 7.02e-25

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


:

Pssm-ID: 396791  Cd Length: 114  Bit Score: 96.98  E-value: 7.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483972  73 QMYFKQPGSRTTCHIENQAIGSLNLNLGPGKCIWYAVASEHSAKFEQLLMKKNLW-PYDSVLWPN----EEELLNWGIPV 147
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGeQPDDLLHLNtiisPKQLRENGIPV 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1017483972 148 MKFIQETDDTVYVGTGTYHWVQSIGFTGNVSWN 180
Cdd:pfam02373  81 YRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVN 113
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 73-180 7.02e-25

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 96.98  E-value: 7.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483972  73 QMYFKQPGSRTTCHIENQAIGSLNLNLGPGKCIWYAVASEHSAKFEQLLMKKNLW-PYDSVLWPN----EEELLNWGIPV 147
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGeQPDDLLHLNtiisPKQLRENGIPV 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1017483972 148 MKFIQETDDTVYVGTGTYHWVQSIGFTGNVSWN 180
Cdd:pfam02373  81 YRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVN 113
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 48-102 4.06e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 40.70  E-value: 4.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1017483972   48 LPNFLKTKGGLNEYIKESIGGVN-EVQMYFKQPGSRTTCHIENQaiGSLNLNLGPG 102
Cdd:smart00558   4 NLAKLPFKLNLLSDLPEDIPGPDvGPYLYMGMAGSTTPWHIDDY--DLVNYLHQGA 57
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 73-180 7.02e-25

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 96.98  E-value: 7.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017483972  73 QMYFKQPGSRTTCHIENQAIGSLNLNLGPGKCIWYAVASEHSAKFEQLLMKKNLW-PYDSVLWPN----EEELLNWGIPV 147
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGeQPDDLLHLNtiisPKQLRENGIPV 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1017483972 148 MKFIQETDDTVYVGTGTYHWVQSIGFTGNVSWN 180
Cdd:pfam02373  81 YRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVN 113
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 48-102 4.06e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 40.70  E-value: 4.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1017483972   48 LPNFLKTKGGLNEYIKESIGGVN-EVQMYFKQPGSRTTCHIENQaiGSLNLNLGPG 102
Cdd:smart00558   4 NLAKLPFKLNLLSDLPEDIPGPDvGPYLYMGMAGSTTPWHIDDY--DLVNYLHQGA 57
 
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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