ID   ESA1_YARLI              Reviewed;         469 AA.
AC   Q6C710;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Histone acetyltransferase ESA1;
DE            EC=2.3.1.48;
GN   Name=ESA1; OrderedLocusNames=YALI0E04675g;
OS   Yarrowia lipolytica (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=4952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
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DR   EMBL; CR382131; CAG79133.1; -; Genomic_DNA.
DR   RefSeq; XP_503552.1; -.
DR   GeneID; 2912208; -.
DR   KEGG; yli:YALI0E04675g; -.
DR   HOGENOM; Q6C710; -.
DR   OMA; Q6C710; VLCECDD.
DR   BRENDA; 2.3.1.48; 3602.
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; Complete proteome; Nucleus;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    469       Histone acetyltransferase ESA1.
FT                                /FTId=PRO_0000051561.
FT   COMPBIAS    103    128       Lys-rich.
FT   ACT_SITE    327    327       By similarity.
SQ   SEQUENCE   469 AA;  53908 MW;  50ABF9A067AD9140 CRC64;
     MALAEADLPN GKTNGKASGS EETPAPVQKV DMNVAINELR VGCKVHVEKD GEDRVAEILS
     VQMRRGNLEF YVHYVEFNKR LDERIAATRV DLSQGVIWPE PEKPKKPLSG AAKESSKEKK
     KNPSKKQKLT DSAATTPGAN SEDVMDLDNL QVNGTTQDPD NFNRDEEIEK LRTGGSMTQS
     SHEVARVRNL QRIVLGNHVI EPWYFSPYPI ELTEEDEIYI CDFTLCYFGS KKQFERFRSK
     STLRHPPGNE IYRDEAVSFF EIDGRKQRTW CRNLCLLSKL FLDHKTLYYD VDPFLFYCMT
     RRDEKGHHLV GYFSKEKESA EGYNVACILT LPQYQRHGYG RLLIDFSYAL SKAEGKTGSP
     EKPLSDLGLL SYRAYWADTI IELLMEKGKQ EMTIEDIASV TAMTTTDVLH TLQTYNMLKY
     YKGQHIICLT DSVCEKYEKM LKKRRRKVNS ELLKWKPPVF TAAQLRFAW
//