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Q75BY2

- ESA1_ASHGO

UniProt

Q75BY2 - ESA1_ASHGO

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: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (09 Jan 2013)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Sites

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

    GO - Molecular functioni

    1. H4 histone acetyltransferase activity Source: EnsemblFungi

    GO - Biological processi

    1. chromatin silencing at rDNA Source: EnsemblFungi
    2. DNA repair Source: EnsemblFungi
    3. DNA-templated transcription, elongation 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

    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

    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
    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.

    Sequence similaritiesi

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

    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.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q75BY2-1 [UniParc]FASTAAdd to Basket

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    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...
    MobiDBi 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.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 81 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