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Q75BY2

- ESA1_ASHGO

UniProt

Q75BY2 - ESA1_ASHGO

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Protein
Histone acetyltransferase ESA1
Gene
ESA1, ACR138W
Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - 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].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521 By similarity
Active sitei294 – 2941Nucleophile By similarity
Binding sitei297 – 2971Acetyl-CoA By similarity
Binding sitei332 – 3321Acetyl-CoA By similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: EnsemblFungi
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: EnsemblFungi
  2. DNA-templated transcription, elongation Source: EnsemblFungi
  3. chromatin silencing at rDNA Source: EnsemblFungi
  4. positive regulation of transcription elongation from RNA polymerase II promoter Source: EnsemblFungi
  5. regulation of cell cycle Source: EnsemblFungi
  6. regulation of transcription by chromatin organization 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:2.3.1.48)
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 ESA1
PRO_0000051551Add
BLAST

Amino acid modifications

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni302 – 3087Acetyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi235 – 25622ESA1-RPD3 motif By similarity
Add
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.

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
KOiK11304.
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.

Sequencei

Sequence statusi: Complete.

Q75BY2-1 [UniParc]FASTAAdd to Basket

« Hide

MAQEEEKDAG ISKYISTTDE IIIGCKCWVE KDGEQRLAEI LSINNRRQPP    50
KFYVHYEDFN KRLDEWILAS RINIEREVTF PKPRDPDEKK KKKQKKSATP 100
QATDGETLES ADIMDLENLN VQGLRDEGIS RDDEIKKLRT SGSMTQNPHE 150
VSRVRNLSKI IMGKHEIEPW YFSPYPIELT DEDVVYIDDF SLQYFGSKKQ 200
YARYRQKCTL RHPPGNEIYR DDYVSFFEID GRKQRTWCRN LCLLSKLFLD 250
HKTLYYDVDP FLFYCMTQRD ELGHHLVGYF SKEKESADGY NVACILTLPQ 300
YQRMGYGRLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLIKL 350
LVENGTEITI DEISSMTSLT TTDILHTAKA LNILRYYKGQ HILYLNEDVL 400
LRYEKLIAKK RRSIDPEKLI WKPPIFTASQ LRFAW 435
Length:435
Mass (Da):51,121
Last modified:January 9, 2013 - v2
Checksum:i7D9F15FADFBB9038
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016816 Genomic DNA. Translation: AAS51364.2.
RefSeqiNP_983540.2. NM_208893.2.

Genome annotation databases

GeneIDi4619672.
KEGGiago:AGOS_ACR138W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016816 Genomic DNA. Translation: AAS51364.2 .
RefSeqi NP_983540.2. NM_208893.2.

3D structure databases

ModBasei Search...

Protein-protein interaction databases

STRINGi 33169.AGOS_ACR138W.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4619672.
KEGGi ago:AGOS_ACR138W.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000182457.
KOi K11304.
OrthoDBi EOG7RFTRR.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

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: April 16, 2014
This is version 80 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

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