ID   ESA1_GIBZE              Reviewed;         502 AA.
AC   Q4IEV4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Histone acetyltransferase ESA1;
DE            EC=2.3.1.48;
GN   Name=ESA1; ORFNames=FG04254;
OS   Gibberella zeae (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella.
OX   NCBI_TaxID=5518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
CC   -!- FUNCTION: Catalytic component of the NuA4 histone
CC       acetyltransferase (HAT) complex which is involved in epigenetic
CC       transcriptional activation of selected genes principally by
CC       acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A
CC       variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac,
CC       H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to
CC       form H2BK16ac, and histone H2A to form H2AK4ac and H2AK7ac.
CC       Acetylation of histone H4 is essential for DNA double-strand break
CC       repair through homologous recombination. Involved in cell cycle
CC       progression. Recruitment to promoters depends on H3K4me (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The ESA1-RPD3 motif is common to ESA1 and RPD3 and is
CC       required for ESA1 histone acetyl-transferase (HAT) activity and
CC       RPD3 histone deacetylase (HDAC) activity.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
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DR   EMBL; AACM01000185; EAA73580.1; -; Genomic_DNA.
DR   RefSeq; XP_384430.1; -.
DR   GeneID; 2786341; -.
DR   KEGG; fgr:FG04254.1; -.
DR   BRENDA; 2.3.1.48; 74326.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR002717; MOZ_SAS.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   SMART; SM00298; CHROMO; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Nucleus; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    502       Histone acetyltransferase ESA1.
FT                                /FTId=PRO_0000051557.
FT   MOTIF       299    320       ESA1-RPD3 motif (By similarity).
FT   ACT_SITE    358    358       By similarity.
FT   BINDING     361    361       Coenzyme A (By similarity).
FT   BINDING     396    396       Coenzyme A (By similarity).
SQ   SEQUENCE   502 AA;  58095 MW;  61DCF761F2C3CD43 CRC64;
     MAGGTPGGEP TVGSGEPRLK SLATPETIKT GCIAWVEKEG QPRRAEILSI KTTKSGKQFY
     CNFDNFNKRL DEWVPVIRLD FTREVEWPNP EKEKPKDPKA KKAPTVQSKK TQPSKKSQKR
     PSKREQSTTS EANTPHPWTD FVENQNRQKS ASIGPDGDSQ ARASVDGGET PGGGDEMEVD
     ERETEVKREP AEFSREVEIE KLRTSGSMTQ NPTEVSRIRN ISKVQFGRFD LYPWYFSPYP
     EIFSQEDVIF ICEFCLSYYG DLKAFTRHRK KCTLQHPPGN ELYRNEEISF FEIDGRRQRT
     WCRNLCLLSK MFLDHKTLYY DVDPFLFYVM TVRTEKGCHM VGYFSKEKES ADGYNVACIL
     TMPQYQRKGY GRLLIQFSYE LSRIEGKLGS PEKPLSDLGL LSYRQYWSEN ILEFLMGYNE
     RDEKVTIEAI STALAMTTQD VEHTLQALRM QVYHKSDHKI VIPEKLIEQR EKTKLKRKRT
     VDPTKIQWKP PVFTASSRTW GW
//