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Conserved domains on  [gi|74870606|sp|Q9VRN3|]
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RecName: Full=Chromatin modification-related protein MEAF6; AltName: Full=Esa1-associated factor 6

Protein Classification

chromatin modification-related protein EAF6/MEAF6( domain architecture ID 10558554)

chromatin modification-related protein EAF6/MEAF6 is a component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A

Gene Ontology:  GO:0035267|GO:0006338|GO:0006351
PubMed:  14966270

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NuA4 pfam09340
Histone acetyltransferase subunit NuA4; The NuA4 histone acetyltransferase (HAT) multisubunit ...
 37-116 2.39e-31

Histone acetyltransferase subunit NuA4; The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. NuA4 complexes are highly conserved in eukaryotes and play primary roles in transcription, cellular response to DNA damage, and cell cycle control.


:

Pssm-ID: 462763  Cd Length: 78  Bit Score: 109.92  E-value: 2.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74870606    37 ELADLIKKKAETSEQLANLERQIYAFEGSYLEDTQLCGNIIRGWERYLTSNkaTNSKADKRNRKFKEAERLFSKSSITSM 116
Cdd:pfam09340   1 ELKELLAKKRELEKELAALEEQIYDKETEYLEETSPGGNIIKGFDGYLKSS--TSAAAGRRKRKFTDEDRIFSLSSVTSP 78
 
Name Accession Description Interval E-value
NuA4 pfam09340
Histone acetyltransferase subunit NuA4; The NuA4 histone acetyltransferase (HAT) multisubunit ...
 37-116 2.39e-31

Histone acetyltransferase subunit NuA4; The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. NuA4 complexes are highly conserved in eukaryotes and play primary roles in transcription, cellular response to DNA damage, and cell cycle control.


Pssm-ID: 462763  Cd Length: 78  Bit Score: 109.92  E-value: 2.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74870606    37 ELADLIKKKAETSEQLANLERQIYAFEGSYLEDTQLCGNIIRGWERYLTSNkaTNSKADKRNRKFKEAERLFSKSSITSM 116
Cdd:pfam09340   1 ELKELLAKKRELEKELAALEEQIYDKETEYLEETSPGGNIIKGFDGYLKSS--TSAAAGRRKRKFTDEDRIFSLSSVTSP 78
 
Name Accession Description Interval E-value
NuA4 pfam09340
Histone acetyltransferase subunit NuA4; The NuA4 histone acetyltransferase (HAT) multisubunit ...
 37-116 2.39e-31

Histone acetyltransferase subunit NuA4; The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. NuA4 complexes are highly conserved in eukaryotes and play primary roles in transcription, cellular response to DNA damage, and cell cycle control.


Pssm-ID: 462763  Cd Length: 78  Bit Score: 109.92  E-value: 2.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74870606    37 ELADLIKKKAETSEQLANLERQIYAFEGSYLEDTQLCGNIIRGWERYLTSNkaTNSKADKRNRKFKEAERLFSKSSITSM 116
Cdd:pfam09340   1 ELKELLAKKRELEKELAALEEQIYDKETEYLEETSPGGNIIKGFDGYLKSS--TSAAAGRRKRKFTDEDRIFSLSSVTSP 78
 
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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