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Q4WHG1

- ESA1_ASPFU

UniProt

Q4WHG1 - ESA1_ASPFU

Protein

Histone acetyltransferase esa1

Gene

esa1

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (05 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, 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 sitei295 – 2951By similarity
    Active sitei337 – 3371NucleophileBy similarity
    Binding sitei340 – 3401Acetyl-CoABy similarity
    Binding sitei375 – 3751Acetyl-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
    ORF Names:AFUA_2G05530
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: 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 – 483483Histone acetyltransferase esa1PRO_0000051552Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei295 – 2951N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-295 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

    STRINGi5085.CADAFUAP00003874.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WHG1.
    SMRiQ4WHG1. Positions 9-67, 196-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini195 – 471277MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni345 – 3517Acetyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi278 – 29922ESA1-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.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 2 hits.
    SSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q4WHG1-1 [UniParc]FASTAAdd to Basket

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    MLLLMFALLQ DGELRKAEIL SIRQRKDGPS FYVHYVDFNK RLDEWIDASR    50
    LDLSHEVEWP QPEKPEKKKT GVGNKAPSKN AQKRARADSR DVSATPDLLT 100
    GKNVNVGKAQ RPSKAGGKEN RDGTPLSMPI VTAEAISTDG TPKAESDDVE 150
    MVDVSFTDGK SIKEEERALG LMSREEEIER LRTSGSMTQN PTEIHRVRNL 200
    NRLQMGKYDI EPWYFSPYPA SFSDADIIYI DEFCLSYFDD KRAFERHRTK 250
    CTLVHPPGNE IYRDDYISFF EVDGRRQRTW CRNLCLLSKL FLDHKTLYYD 300
    VDPFLFYCMC TRDETGCHLV GYFSKEKDSA EGYNLACILT LPQYQRRGFG 350
    RLLISFSYEL SKREGKLGSP EKPLSDLGLL GYRQYWRETL VEILMEPGRE 400
    TVSENELALL TSMTEKDVHE TLVVLNMLRY YKGNWVIVLT DYVVEQHKKR 450
    LEKEKLKGAR KIDPARLQWK PPVFTASSRT WNW 483
    Length:483
    Mass (Da):55,969
    Last modified:July 5, 2005 - v1
    Checksum:i8EBF3CDAE55CE6F8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87644.1.
    RefSeqiXP_749682.1. XM_744589.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00003874; CADAFUAP00003874; CADAFUAG00003874.
    GeneIDi3506677.
    KEGGiafm:AFUA_2G05530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87644.1 .
    RefSeqi XP_749682.1. XM_744589.1.

    3D structure databases

    ProteinModelPortali Q4WHG1.
    SMRi Q4WHG1. Positions 9-67, 196-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00003874.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00003874 ; CADAFUAP00003874 ; CADAFUAG00003874 .
    GeneIDi 3506677.
    KEGGi afm:AFUA_2G05530.

    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.
    [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. 2 hits.
    SSF55729. SSF55729. 1 hit.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiESA1_ASPFU
    AccessioniPrimary (citable) accession number: Q4WHG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: July 5, 2005
    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