ID   ESA1_USTMA              Reviewed;         565 AA.
AC   Q4P3S3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, 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; ORFNames=UM05240;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
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, and histone H2A
CC       to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is
CC       essential for DNA double-strand break repair through homologous
CC       recombination. Involved in cell cycle progression. Recruitment to
CC       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; AACP01000190; EAK82853.1; -; Genomic_DNA.
DR   RefSeq; XP_761387.1; -.
DR   GeneID; 3633352; -.
DR   KEGG; uma:UM05240.1; -.
DR   OMA; Q4P3S3; DPFLYYC.
DR   BRENDA; 2.3.1.48; 2320.
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:0008270; F:zinc ion binding; IEA:InterPro.
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   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
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   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Complete proteome; Nucleus;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    565       Histone acetyltransferase ESA1.
FT                                /FTId=PRO_0000051560.
FT   MOTIF       367    388       ESA1-RPD3 motif (By similarity).
FT   ACT_SITE    426    426       By similarity.
FT   BINDING     429    429       Coenzyme A (By similarity).
FT   BINDING     464    464       Coenzyme A (By similarity).
SQ   SEQUENCE   565 AA;  63408 MW;  C35F30CBD96EB754 CRC64;
     MAPRTQKSTS GTPGGSGTPG PDEGPQISPG GTYGLEDVVV GCKAFVQKPD VVTGEMEERK
     AEILSIREKP KPRLTKKQQA ELADKPAPTL EETLEYYVHY CEFNKRLDEW VSGTRLITSR
     ELEWPKKEVT SDKTKRKVIR AGSGATTPST PLTPTGKGYR GAGASNLLKK AAAQAAKNVQ
     GESGLETPQK RKADSGDTST AQSIRADSID ADADGEDDEN GAVVAMEMLG GNDQQEKDDV
     ATESNGGLTA SLNANQGQET FSKKQEIEKL RTSGSMTQSV SEVARVKNLN KIQMGKSEVE
     TWYFSPYPLE YAHIDTLYIC EMCLSYFPSP FTLKRHRSKC TLLHPPGNEI YRHEDISFFE
     IDGRLQRTWC RNLCLLSKCF LDHKTLYYDV DPFLYYCMVK RDDLGCHLLG YFSKEKDSAE
     NYNVACILTL PQHQRAGYGK LLIEFSYELT KIEGKLGSPE KPLSDLGLLS YRAYWAEIIV
     ELLLKTEDEI SIEEIAQKTA FTHADILHTC MALNMLKQYQ GKHMIVLSDL IISKYTAKRP
     RKRINPQKLH WTAKNWHRSQ LNFGW
//