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Q6FPH9

- ESA1_CANGA

UniProt

Q6FPH9 - ESA1_CANGA

Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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      Entry version 70 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      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, and histone H2A to form H2AK4ac and H2AK7ac. 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 sitei263 – 2631By similarity
    Active sitei305 – 3051NucleophileBy similarity
    Binding sitei308 – 3081Acetyl-CoABy similarity
    Binding sitei343 – 3431Acetyl-CoABy similarity

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    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:CAGL0J03696g
    OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
    Taxonomic identifieri284593 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces
    ProteomesiUP000002428: Chromosome J

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446Histone acetyltransferase ESA1PRO_0000051554Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei263 – 2631N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-263 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FPH9.
    SMRiQ6FPH9. Positions 7-90, 163-435.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini163 – 434272MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni313 – 3197Acetyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi246 – 26722ESA1-RPD3 motifBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi94 – 1018Poly-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

    HOGENOMiHOG000182457.
    KOiK11304.
    OMAiSQLRFAW.
    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.

    Q6FPH9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAEVEEEA GIPKKIESTE EVLIKCQCWV RKDEEERLAE ILSINARVSP    50
    SKFYVHYVNF NKRLDEWVTG DRINLDKEVI FPRPKRQLEE DTNKKQKKKK 100
    KFPQKAAVVE SDAKSSEMGE GSDVMDLDNL NVRGLKDEEI SREDEIKKLR 150
    TSGSMIQNPH EVAHVRNLSK IIMGKFEIEP WYFSPYPIEL TDLDVVYIDD 200
    FTLQYFGSRK QYERYRKKCT LRHPPGNEIY RDDYVSFFEI DGRKQRTWCR 250
    NLCLLSKLFL DHKTLYYDVD PFLFYCMTRR DEMGHHFVGY FSKEKESADG 300
    YNVACILTLP QYQRMGYGRL LIEFSYELSK KEGKVGSPEK PLSDLGLLSY 350
    RAYWSDVLIT LLVEHGKEVT IDEISSMTSM TTTDILHTLK TLNILRYYKG 400
    QHIIFLNDDI LERYNQLKTK KRRHIDAEKL LWKPPVFTAS QLRFAW 446
    Length:446
    Mass (Da):52,552
    Last modified:July 19, 2004 - v1
    Checksum:i8E5A7B01F9D4CD94
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR380956 Genomic DNA. Translation: CAG60814.1.
    RefSeqiXP_447865.1. XM_447865.1.

    Genome annotation databases

    GeneIDi2889685.
    KEGGicgr:CAGL0J03696g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR380956 Genomic DNA. Translation: CAG60814.1 .
    RefSeqi XP_447865.1. XM_447865.1.

    3D structure databases

    ProteinModelPortali Q6FPH9.
    SMRi Q6FPH9. Positions 7-90, 163-435.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2889685.
    KEGGi cgr:CAGL0J03696g.

    Phylogenomic databases

    HOGENOMi HOG000182457.
    KOi K11304.
    OMAi SQLRFAW.
    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...

    Entry informationi

    Entry nameiESA1_CANGA
    AccessioniPrimary (citable) accession number: Q6FPH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 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