ID   ESA1_CANGA              Reviewed;         446 AA.
AC   Q6FPH9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Histone acetyltransferase ESA1;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q08649};
DE   AltName: Full=Protein 2-hydroxyisobutyryltransferase ESA1 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:O94446};
DE   AltName: Full=Protein acetyltransferase ESA1 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q08649};
DE   AltName: Full=Protein crotonyltransferase ESA1 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q08649};
GN   Name=ESA1; OrderedLocusNames=CAGL0J03696g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalytic component of the NuA4 histone acetyltransferase
CC       (HAT) complex which is involved in epigenetic transcriptional
CC       activation of selected genes principally by acetylation of nucleosomal
CC       histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity).
CC       Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac,
CC       histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac
CC       (By similarity). The NuA4 complex is involved in the DNA damage
CC       response and is required for chromosome segregation. The NuA4 complex
CC       plays a direct role in repair of DNA double-strand breaks (DSBs)
CC       through homologous recombination (By similarity). Recruitment to
CC       promoters depends on H3K4me. Also acetylates non-histone proteins (By
CC       similarity). In addition to protein acetyltransferase, can use
CC       different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-
CC       hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able
CC       to mediate protein 2-hydroxyisobutyrylation and crotonylation,
CC       respectively (By similarity). {ECO:0000250|UniProtKB:O94446,
CC       ECO:0000250|UniProtKB:Q08649}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC         Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:O94446};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000250|UniProtKB:O94446};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000250|UniProtKB:Q08649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC         Evidence={ECO:0000250|UniProtKB:Q08649};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC         N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC         ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:O94446};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC         Evidence={ECO:0000250|UniProtKB:O94446};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC         (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q08649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC         Evidence={ECO:0000250|UniProtKB:Q08649};
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC       {ECO:0000250|UniProtKB:Q08649}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94446}.
CC       Chromosome {ECO:0000250|UniProtKB:O94446}. Note=Following DNA damage,
CC       localizes to sites of DNA damage, such as double stand breaks (DSBs).
CC       {ECO:0000250|UniProtKB:O94446}.
CC   -!- DOMAIN: The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required
CC       for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone
CC       deacetylase (HDAC) activity. {ECO:0000250|UniProtKB:Q08649}.
CC   -!- PTM: Autoacetylation at Lys-263 is required for proper function.
CC       {ECO:0000250|UniProtKB:Q08649}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR   EMBL; CR380956; CAG60814.1; -; Genomic_DNA.
DR   RefSeq; XP_447865.1; XM_447865.1.
DR   AlphaFoldDB; Q6FPH9; -.
DR   SMR; Q6FPH9; -.
DR   STRING; 284593.Q6FPH9; -.
DR   EnsemblFungi; CAGL0J03696g-T; CAGL0J03696g-T-p1; CAGL0J03696g.
DR   GeneID; 2889685; -.
DR   KEGG; cgr:CAGL0J03696g; -.
DR   CGD; CAL0129567; CAGL0J03696g.
DR   VEuPathDB; FungiDB:B1J91_J03696g; -.
DR   VEuPathDB; FungiDB:CAGL0J03696g; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_0_1; -.
DR   InParanoid; Q6FPH9; -.
DR   OMA; QYQRHGY; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR   GO; GO:0044016; F:histone H3K4 acetyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR   GO; GO:0140065; F:peptide butyryltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:EnsemblFungi.
DR   GO; GO:0031453; P:positive regulation of heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR025995; Tudor-knot.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   3: Inferred from homology;
KW   Acetylation; Activator; Chromatin regulator; Chromosome; DNA damage;
KW   DNA repair; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..446
FT                   /note="Histone acetyltransferase ESA1"
FT                   /id="PRO_0000051554"
FT   DOMAIN          24..75
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          163..434
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         196..221
FT                   /note="C2HC MYST-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          86..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           246..267
FT                   /note="ESA1-RPD3 motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        86..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        339
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         304..308
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         313..319
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         343
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   SITE            305
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   MOD_RES         263
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
SQ   SEQUENCE   446 AA;  52552 MW;  8E5A7B01F9D4CD94 CRC64;
     MAGAEVEEEA GIPKKIESTE EVLIKCQCWV RKDEEERLAE ILSINARVSP SKFYVHYVNF
     NKRLDEWVTG DRINLDKEVI FPRPKRQLEE DTNKKQKKKK KFPQKAAVVE SDAKSSEMGE
     GSDVMDLDNL NVRGLKDEEI SREDEIKKLR TSGSMIQNPH EVAHVRNLSK IIMGKFEIEP
     WYFSPYPIEL TDLDVVYIDD FTLQYFGSRK QYERYRKKCT LRHPPGNEIY RDDYVSFFEI
     DGRKQRTWCR NLCLLSKLFL DHKTLYYDVD PFLFYCMTRR DEMGHHFVGY FSKEKESADG
     YNVACILTLP QYQRMGYGRL LIEFSYELSK KEGKVGSPEK PLSDLGLLSY RAYWSDVLIT
     LLVEHGKEVT IDEISSMTSM TTTDILHTLK TLNILRYYKG QHIIFLNDDI LERYNQLKTK
     KRRHIDAEKL LWKPPVFTAS QLRFAW
//