ID   ESA1_CRYNE              Reviewed;         564 AA.
AC   Q5KM33; Q55XW1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Histone acetyltransferase ESA1;
DE            EC=2.3.1.48;
GN   Name=ESA1; OrderedLocusNames=CNB03160, CNBB2530;
OS   Cryptococcus neoformans (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella;
OC   Filobasidiella/Cryptococcus neoformans species complex.
OX   NCBI_TaxID=5207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A, and JEC21;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J.,
RA   D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J.,
RA   Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I.,
RA   Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E.,
RA   Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L.,
RA   Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A.,
RA   Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R.,
RA   Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W.,
RA   Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen
RT   Cryptococcus neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017342; AAW41586.1; -; Genomic_DNA.
DR   EMBL; AAEY01000009; EAL22621.1; -; Genomic_DNA.
DR   RefSeq; XP_568893.1; -.
DR   RefSeq; XP_777268.1; -.
DR   UniGene; Fne.2644; -.
DR   UniGene; Fne.5908; -.
DR   GeneID; 3255895; -.
DR   GeneID; 4934345; -.
DR   GenomeReviews; AE017342_GR; CNB03160.
DR   KEGG; cnb:CNBB2530; -.
DR   KEGG; cne:CNB03160; -.
DR   HOGENOM; Q5KM33; -.
DR   OMA; Q5KM33; DPFLYYC.
DR   BRENDA; 2.3.1.48; 2772.
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; 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   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    564       Histone acetyltransferase ESA1.
FT                                /FTId=PRO_0000051555.
FT   MOTIF       364    385       ESA1-RPD3 motif (By similarity).
FT   COMPBIAS     65     85       Pro-rich.
FT   COMPBIAS    121    199       Lys-rich.
FT   ACT_SITE    423    423       By similarity.
FT   BINDING     426    426       Coenzyme A (By similarity).
FT   BINDING     461    461       Coenzyme A (By similarity).
SQ   SEQUENCE   564 AA;  63050 MW;  76BE79DB995BF692 CRC64;
     MSPSAPSTPH GRGSGSEPGT PAPSVAAGGS YTIDDVVPGV KIYVIKPLSN GQAEQRRAEI
     LSTRPKPKPS AFAPPPPPNA PSPDPRDDTE YYVHYVEFNK RLDEWVGGSR LVLSKEMEWP
     KSKDEPKKKD RPAKAQPSKA PSRATGSPIP SDSLLKKAAN KAAMAAGKAT PGKAMPSSKL
     GKASKIGKAG KFPQKRKAKT EADTEAEEES NEDNDALGEE EDMDEDGDVT LITSDGAIDP
     SREVVAAPSN PRAAPQVFSK KQEIEKLRTS GSMTQSHSEI SRVKNLNKLQ IGKHEVETWY
     FSPYPIEYAH LPVLYICEFC LLYYPSATQL RRHRAKCTLL HPPGNEIYRH EGISFFEIDG
     RKQRTWCRNL CLISKCFLDH KTLYYDVDPF LYYCMTVKDD YGCHLIGYFS KEKESAEGYN
     VACILTLPQH QRKGYGRLLI EFSYELSKVE GKLGSPEKPL SDLGLLGYRA YWQEKIVELL
     LDSDYEISLD EIAQKTSITH GDIMHTCQAL QMIKYYKNSH IIHLTDAVIE QHKKTKAKPR
     RAINPAYLKW KPPVFSRAQL AFGF
//