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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei294 – 2941Important for catalytic activityBy similarity
Active sitei328 – 3281Proton donor/acceptorBy similarity
Binding sitei332 – 3321Acetyl-CoABy similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: EnsemblFungi

GO - Biological processi

  1. chromatin organization involved in regulation of transcription Source: EnsemblFungi
  2. chromatin silencing at rDNA Source: EnsemblFungi
  3. DNA repair Source: EnsemblFungi
  4. DNA-templated transcription, elongation Source: EnsemblFungi
  5. positive regulation of transcription elongation from RNA polymerase II promoter Source: EnsemblFungi
  6. regulation of cell cycle Source: EnsemblFungi
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase ESA1 (EC:2.3.1.48By similarity)
Gene namesi
Name:ESA1
Ordered Locus Names:ACR138W
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
ProteomesiUP000000591: Chromosome III

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. Piccolo NuA4 histone acetyltransferase complex Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Histone acetyltransferase ESA1PRO_0000051551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex.By similarity

Protein-protein interaction databases

STRINGi33169.AGOS_ACR138W.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 423272MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni293 – 2975Acetyl-CoA bindingBy similarity
Regioni302 – 3087Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi235 – 25622ESA1-RPD3 motifBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi89 – 968Poly-Lys

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ75BY2.
KOiK11304.
OMAiGCIAMVE.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q75BY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQEEEKDAG ISKYISTTDE IIIGCKCWVE KDGEQRLAEI LSINNRRQPP
60 70 80 90 100
KFYVHYEDFN KRLDEWILAS RINIEREVTF PKPRDPDEKK KKKQKKSATP
110 120 130 140 150
QATDGETLES ADIMDLENLN VQGLRDEGIS RDDEIKKLRT SGSMTQNPHE
160 170 180 190 200
VSRVRNLSKI IMGKHEIEPW YFSPYPIELT DEDVVYIDDF SLQYFGSKKQ
210 220 230 240 250
YARYRQKCTL RHPPGNEIYR DDYVSFFEID GRKQRTWCRN LCLLSKLFLD
260 270 280 290 300
HKTLYYDVDP FLFYCMTQRD ELGHHLVGYF SKEKESADGY NVACILTLPQ
310 320 330 340 350
YQRMGYGRLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLIKL
360 370 380 390 400
LVENGTEITI DEISSMTSLT TTDILHTAKA LNILRYYKGQ HILYLNEDVL
410 420 430
LRYEKLIAKK RRSIDPEKLI WKPPIFTASQ LRFAW
Length:435
Mass (Da):51,121
Last modified:January 9, 2013 - v2
Checksum:i7D9F15FADFBB9038
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016816 Genomic DNA. Translation: AAS51364.2.
RefSeqiNP_983540.2. NM_208893.2.

Genome annotation databases

EnsemblFungiiAAS51364; AAS51364; AGOS_ACR138W.
GeneIDi4619672.
KEGGiago:AGOS_ACR138W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016816 Genomic DNA. Translation: AAS51364.2.
RefSeqiNP_983540.2. NM_208893.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi33169.AGOS_ACR138W.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS51364; AAS51364; AGOS_ACR138W.
GeneIDi4619672.
KEGGiago:AGOS_ACR138W.

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ75BY2.
KOiK11304.
OMAiGCIAMVE.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiESA1_ASHGO
AccessioniPrimary (citable) accession number: Q75BY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 9, 2013
Last modified: March 4, 2015
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.