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Q75BY2 (ESA1_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase ESA1

EC=2.3.1.48
Gene names
Name:ESA1
Ordered Locus Names:ACR138W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me By similarity.

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Subunit structure

Component of the NuA4 histone acetyltransferase complex By similarity.

Subcellular location

Nucleus By similarity.

Domain

The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.

Post-translational modification

Autoacetylation at Lys-252 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435Histone acetyltransferase ESA1
PRO_0000051551

Regions

Region302 – 3087Acetyl-CoA binding By similarity
Motif235 – 25622ESA1-RPD3 motif By similarity
Compositional bias89 – 968Poly-Lys

Sites

Active site2521 By similarity
Active site2941Nucleophile By similarity
Binding site2971Acetyl-CoA By similarity
Binding site3321Acetyl-CoA By similarity

Amino acid modifications

Modified residue2521N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q75BY2 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: 7D9F15FADFBB9038

FASTA43551,121
        10         20         30         40         50         60 
MAQEEEKDAG ISKYISTTDE IIIGCKCWVE KDGEQRLAEI LSINNRRQPP KFYVHYEDFN 

        70         80         90        100        110        120 
KRLDEWILAS RINIEREVTF PKPRDPDEKK KKKQKKSATP QATDGETLES ADIMDLENLN 

       130        140        150        160        170        180 
VQGLRDEGIS RDDEIKKLRT SGSMTQNPHE VSRVRNLSKI IMGKHEIEPW YFSPYPIELT 

       190        200        210        220        230        240 
DEDVVYIDDF SLQYFGSKKQ YARYRQKCTL RHPPGNEIYR DDYVSFFEID GRKQRTWCRN 

       250        260        270        280        290        300 
LCLLSKLFLD HKTLYYDVDP FLFYCMTQRD ELGHHLVGYF SKEKESADGY NVACILTLPQ 

       310        320        330        340        350        360 
YQRMGYGRLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLIKL LVENGTEITI 

       370        380        390        400        410        420 
DEISSMTSLT TTDILHTAKA LNILRYYKGQ HILYLNEDVL LRYEKLIAKK RRSIDPEKLI 

       430 
WKPPIFTASQ LRFAW 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016816 Genomic DNA. Translation: AAS51364.2.
RefSeqNP_983540.2. NM_208893.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_ACR138W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4619672.
KEGGago:AGOS_ACR138W.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OrthoDBEOG7RFTRR.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_ASHGO
AccessionPrimary (citable) accession number: Q75BY2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 9, 2013
Last modified: April 16, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families