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Conserved domains on  [gi|984077148]
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Chain A, HUMAN LYSINE-SPECIFIC DEMETHYLASE 6B, JMJD3

Protein Classification

bifunctional arginine demethylase and lysyl-hydroxylase( domain architecture ID 10651274)

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 ...
 238-346 1.85e-35

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: 128.18  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984077148  238 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHG-------VDYLTGSWWPILddLYASNI 310
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISPKQ--LRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 984077148  311 PVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNV 346
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 204-268 1.33e-07

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: 48.40  E-value: 1.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984077148   204 QLQELLKLPafmrvtSTGNMLSHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 268
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 ...
 238-346 1.85e-35

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: 128.18  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984077148  238 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHG-------VDYLTGSWWPILddLYASNI 310
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISPKQ--LRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 984077148  311 PVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNV 346
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 204-268 1.33e-07

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: 48.40  E-value: 1.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984077148   204 QLQELLKLPafmrvtSTGNMLSHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 268
Cdd:smart00558   1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
246-337 4.99e-03

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 36.75  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984077148 246 SRTPGHQENNNFCSVNINIGPGdcEWFAVHEHYWETIsAFCdrhgvdyLTGSWWPILDDlyasniPVYRFvqRPGDLVWI 325
Cdd:COG1917   12 SVRVLADGEDELEVVRVTFEPG--ARTPWHSHPGEEL-IYV-------LEGEGEVEVGG------EEYEL--KPGDVVFI 73

                         90
                 ....*....|..
gi 984077148 326 NAGTVHWVQATG 337
Cdd:COG1917   74 PPGVPHAFRNLG 85
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 238-346 1.85e-35

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: 128.18  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984077148  238 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHG-------VDYLTGSWWPILddLYASNI 310
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISPKQ--LRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 984077148  311 PVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNV 346
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 204-268 1.33e-07

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: 48.40  E-value: 1.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984077148   204 QLQELLKLPafmrvtSTGNMLSHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 268
Cdd:smart00558   1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
246-337 4.99e-03

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 36.75  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984077148 246 SRTPGHQENNNFCSVNINIGPGdcEWFAVHEHYWETIsAFCdrhgvdyLTGSWWPILDDlyasniPVYRFvqRPGDLVWI 325
Cdd:COG1917   12 SVRVLADGEDELEVVRVTFEPG--ARTPWHSHPGEEL-IYV-------LEGEGEVEVGG------EEYEL--KPGDVVFI 73

                         90
                 ....*....|..
gi 984077148 326 NAGTVHWVQATG 337
Cdd:COG1917   74 PPGVPHAFRNLG 85
 
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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