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P0CP03

- ESA1_CRYNB

UniProt

P0CP03 - ESA1_CRYNB

Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 18 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      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, 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 sitei381 – 3811By similarity
    Active sitei423 – 4231NucleophileBy similarity
    Binding sitei426 – 4261Acetyl-CoABy similarity
    Binding sitei461 – 4611Acetyl-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:CNBB2530
    OrganismiCryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans)
    Taxonomic identifieri283643 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
    ProteomesiUP000001435: Chromosome 2

    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 – 564564Histone acetyltransferase ESA1PRO_0000410158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei381 – 3811N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-381 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

    ProteinModelPortaliP0CP03.
    SMRiP0CP03. Positions 281-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini281 – 552272MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni431 – 4377Acetyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi364 – 38522ESA1-RPD3 motifBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi65 – 8521Pro-richAdd
    BLAST
    Compositional biasi121 – 19979Lys-richAdd
    BLAST

    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.
    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.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0CP03-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPSAPSTPH GRGSGSEPGT PAPSVAAGGS YTIDDVVPGV KIYVIKPLSN    50
    GQAEQRRAEI LSTRPKPKPS AFAPPPPPNA PSPDPRDDTE YYVHYVEFNK 100
    RLDEWVGGSR LVLSKEMEWP KSKDEPKKKD RPAKAQPSKA PSRATGSPIP 150
    SDSLLKKAAN KAAMAAGKAT PGKAMPSSKL GKASKIGKAG KFPQKRKAKT 200
    EADTEAEEES NEDNDALGEE EDMDEDGDVT LITSDGAIDP SREVVAAPSN 250
    PRAAPQVFSK KQEIEKLRTS GSMTQSHSEI SRVKNLNKLQ IGKHEVETWY 300
    FSPYPIEYAH LPVLYICEFC LLYYPSATQL RRHRAKCTLL HPPGNEIYRH 350
    EGISFFEIDG RKQRTWCRNL CLISKCFLDH KTLYYDVDPF LYYCMTVKDD 400
    YGCHLIGYFS KEKESAEGYN VACILTLPQH QRKGYGRLLI EFSYELSKVE 450
    GKLGSPEKPL SDLGLLGYRA YWQEKIVELL LDSDYEISLD EIAQKTSITH 500
    GDIMHTCQAL QMIKYYKNSH IIHLTDAVIE QHKKTKAKPR RAINPAYLKW 550
    KPPVFSRAQL AFGF 564
    Length:564
    Mass (Da):63,050
    Last modified:June 28, 2011 - v1
    Checksum:i76BE79DB995BF692
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEY01000009 Genomic DNA. Translation: EAL22621.1.
    RefSeqiXP_777268.1. XM_772175.1.

    Genome annotation databases

    GeneIDi4934345.
    KEGGicnb:CNBB2530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEY01000009 Genomic DNA. Translation: EAL22621.1 .
    RefSeqi XP_777268.1. XM_772175.1.

    3D structure databases

    ProteinModelPortali P0CP03.
    SMRi P0CP03. Positions 281-553.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4934345.
    KEGGi cnb:CNBB2530.

    Phylogenomic databases

    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.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 1 hit.
    SM00355. ZnF_C2H2. 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 genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
      Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.
      , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.
      Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B-3501A.

    Entry informationi

    Entry nameiESA1_CRYNB
    AccessioniPrimary (citable) accession number: P0CP03
    Secondary accession number(s): Q55XW1, Q5KM33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 18 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3