ID   ESA1_KLULA              Reviewed;         439 AA.
AC   Q6CKE9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Histone acetyltransferase ESA1;
DE            EC=2.3.1.48;
GN   Name=ESA1; OrderedLocusNames=KLLA0F11209g;
OS   Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
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, histone H2A to form H2AK4ac and H2AK7ac, and
CC       histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone
CC       H4 is essential for DNA double-strand break repair through
CC       homologous recombination. Involved in cell cycle progression.
CC       Recruitment to promoters depends on H3K4me (By 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; CR382126; CAG98298.1; -; Genomic_DNA.
DR   RefSeq; XP_455590.1; -.
DR   SMR; Q6CKE9; 156-428.
DR   GeneID; 2895129; -.
DR   KEGG; kla:KLLA0F11209g; -.
DR   HOGENOM; Q6CKE9; -.
DR   OMA; Q6CKE9; VLCECDD.
DR   BRENDA; 2.3.1.48; 74088.
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    439       Histone acetyltransferase ESA1.
FT                                /FTId=PRO_0000051558.
FT   MOTIF       239    260       ESA1-RPD3 motif (By similarity).
FT   ACT_SITE    298    298       By similarity.
FT   BINDING     301    301       Coenzyme A (By similarity).
FT   BINDING     336    336       Coenzyme A (By similarity).
SQ   SEQUENCE   439 AA;  51474 MW;  20E81CA743A33F81 CRC64;
     MSHGEEKEPG IPQKVDSIDE IFVGCKSWVL KDGQDRLAEI LSINSRRDPP KFYVHYEDFN
     KRLDEWITAD RLQIDKEVIF PRPKELEEKK DSKKKKQQQN KSATPQAASA TPDGGDVMDL
     DNLNVQGIPN EDISREDEIK KLRTSGSMTQ NQNEVARVRN LNKVIMGKYE IEPWYFSPYP
     IELTDEDVVY IDDFSLQYFG SKKQYERYRK KCTLRHPPGN EIYRDDYVSF FEIDGRKQRT
     WCRNLCLLSK LFLDHKTLYY DVDPFLFYCM TRRDELGHHI VGYFSKEKES ADAYNVACIL
     TLPQYQRMGY GRLLIEFSYE LSKKEGKVGS PEKPLSDLGL LSYRAYWADT LIKLLVEHGQ
     EITIDEVSSI SSMTTTDILH TAKALEILRF YRGQHVLYLN SDVMKRYKKL KNNKRRSIDP
     QKLIWTPPVF TASQLRFAW
//