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Conserved domains on  [gi|1039799726|ref|XP_017174178|]
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histone demethylase UTY isoform X17 [Mus musculus]

Protein Classification

JmjC domain-containing protein( domain architecture ID 10651274)

JmjC domain-containing protein

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 ...
 482-590 1.08e-33

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: 125.10  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039799726 482 QLCMKVPGSRIPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 554
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039799726 555 PVYRFIQRPGDLVWINAGTVHWVQAIGWCNNITWNV 590
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 448-512 5.04e-04

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: 38.77  E-value: 5.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039799726  448 QLHELTKLPafvrvvSAGNLLSHVGYTILGMNSVQLC-MKVPGSRIPGHQENNNfcSVNINIGPGD 512
Cdd:smart00558   1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVGPYLyMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 482-590 1.08e-33

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: 125.10  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039799726 482 QLCMKVPGSRIPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 554
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039799726 555 PVYRFIQRPGDLVWINAGTVHWVQAIGWCNNITWNV 590
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 448-512 5.04e-04

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: 38.77  E-value: 5.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039799726  448 QLHELTKLPafvrvvSAGNLLSHVGYTILGMNSVQLC-MKVPGSRIPGHQENNNfcSVNINIGPGD 512
Cdd:smart00558   1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVGPYLyMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 482-590 1.08e-33

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: 125.10  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039799726 482 QLCMKVPGSRIPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 554
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039799726 555 PVYRFIQRPGDLVWINAGTVHWVQAIGWCNNITWNV 590
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 448-512 5.04e-04

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: 38.77  E-value: 5.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039799726  448 QLHELTKLPafvrvvSAGNLLSHVGYTILGMNSVQLC-MKVPGSRIPGHQENNNfcSVNINIGPGD 512
Cdd:smart00558   1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVGPYLyMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
 
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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