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Q4P3S3

- ESA1_USTMA

UniProt

Q4P3S3 - ESA1_USTMA

Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      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 sitei384 – 3841By similarity
    Active sitei426 – 4261NucleophileBy similarity
    Binding sitei429 – 4291Acetyl-CoABy similarity
    Binding sitei464 – 4641Acetyl-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
    ORF Names:UM05240
    OrganismiUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
    Taxonomic identifieri237631 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago
    ProteomesiUP000000561: Unassembled WGS sequence

    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 – 565565Histone acetyltransferase ESA1PRO_0000051560Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei384 – 3841N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-384 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

    STRINGi5270.UM05240.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4P3S3.
    SMRiQ4P3S3. Positions 284-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini284 – 553270MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni434 – 4407Acetyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi367 – 38822ESA1-RPD3 motifBy similarityAdd
    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

    eggNOGiCOG5027.
    HOGENOMiHOG000182457.
    KOiK11304.
    OMAiEVEWPAP.
    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.

    Q4P3S3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRTQKSTS GTPGGSGTPG PDEGPQISPG GTYGLEDVVV GCKAFVQKPD    50
    VVTGEMEERK AEILSIREKP KPRLTKKQQA ELADKPAPTL EETLEYYVHY 100
    CEFNKRLDEW VSGTRLITSR ELEWPKKEVT SDKTKRKVIR AGSGATTPST 150
    PLTPTGKGYR GAGASNLLKK AAAQAAKNVQ GESGLETPQK RKADSGDTST 200
    AQSIRADSID ADADGEDDEN GAVVAMEMLG GNDQQEKDDV ATESNGGLTA 250
    SLNANQGQET FSKKQEIEKL RTSGSMTQSV SEVARVKNLN KIQMGKSEVE 300
    TWYFSPYPLE YAHIDTLYIC EMCLSYFPSP FTLKRHRSKC TLLHPPGNEI 350
    YRHEDISFFE IDGRLQRTWC RNLCLLSKCF LDHKTLYYDV DPFLYYCMVK 400
    RDDLGCHLLG YFSKEKDSAE NYNVACILTL PQHQRAGYGK LLIEFSYELT 450
    KIEGKLGSPE KPLSDLGLLS YRAYWAEIIV ELLLKTEDEI SIEEIAQKTA 500
    FTHADILHTC MALNMLKQYQ GKHMIVLSDL IISKYTAKRP RKRINPQKLH 550
    WTAKNWHRSQ LNFGW 565
    Length:565
    Mass (Da):63,408
    Last modified:July 19, 2005 - v1
    Checksum:iC35F30CBD96EB754
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACP01000190 Genomic DNA. Translation: EAK82853.1.
    RefSeqiXP_761387.1. XM_756294.1.

    Genome annotation databases

    EnsemblFungiiUM05240T0; UM05240P0; UM05240.
    GeneIDi3633352.
    KEGGiuma:UM05240.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACP01000190 Genomic DNA. Translation: EAK82853.1 .
    RefSeqi XP_761387.1. XM_756294.1.

    3D structure databases

    ProteinModelPortali Q4P3S3.
    SMRi Q4P3S3. Positions 284-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5270.UM05240.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii UM05240T0 ; UM05240P0 ; UM05240 .
    GeneIDi 3633352.
    KEGGi uma:UM05240.1.

    Phylogenomic databases

    eggNOGi COG5027.
    HOGENOMi HOG000182457.
    KOi K11304.
    OMAi EVEWPAP.
    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. "Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
      Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.
      , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
      Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 521 / FGSC 9021.

    Entry informationi

    Entry nameiESA1_USTMA
    AccessioniPrimary (citable) accession number: Q4P3S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 71 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