ID   ESA1_EREGS              Reviewed;         435 AA.
AC   Q75BY2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 129.
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=ACR138W;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 (By
CC       similarity). Interacts with arp4 (By similarity).
CC       {ECO:0000250|UniProtKB:O94446, ECO:0000250|UniProtKB:Q08649}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94446}.
CC       Chromosome {ECO:0000250|UniProtKB:O94446}. Note=Localizes to
CC       pericentric heterochromatin. Following DNA damage, localizes to sites
CC       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-252 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; AE016816; AAS51364.2; -; Genomic_DNA.
DR   RefSeq; NP_983540.2; NM_208893.2.
DR   AlphaFoldDB; Q75BY2; -.
DR   SMR; Q75BY2; -.
DR   STRING; 284811.Q75BY2; -.
DR   EnsemblFungi; AAS51364; AAS51364; AGOS_ACR138W.
DR   GeneID; 4619672; -.
DR   KEGG; ago:AGOS_ACR138W; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_0_1; -.
DR   InParanoid; Q75BY2; -.
DR   OMA; QYQRHGY; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0000786; C:nucleosome; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032777; C:piccolo histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0140068; F:histone crotonyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006354; P:DNA-templated transcription elongation; IEA:EnsemblFungi.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:EnsemblFungi.
DR   CDD; cd18986; CBD_ESA1_like; 1.
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; 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   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..435
FT                   /note="Histone acetyltransferase ESA1"
FT                   /id="PRO_0000051551"
FT   DOMAIN          22..73
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          152..423
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         185..210
FT                   /note="C2HC MYST-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          78..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           235..256
FT                   /note="ESA1-RPD3 motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        78..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        328
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         293..297
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         302..308
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         332
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   SITE            294
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
SQ   SEQUENCE   435 AA;  51121 MW;  7D9F15FADFBB9038 CRC64;
     MAQEEEKDAG ISKYISTTDE IIIGCKCWVE KDGEQRLAEI LSINNRRQPP KFYVHYEDFN
     KRLDEWILAS RINIEREVTF PKPRDPDEKK KKKQKKSATP QATDGETLES ADIMDLENLN
     VQGLRDEGIS RDDEIKKLRT SGSMTQNPHE VSRVRNLSKI IMGKHEIEPW YFSPYPIELT
     DEDVVYIDDF SLQYFGSKKQ YARYRQKCTL RHPPGNEIYR DDYVSFFEID GRKQRTWCRN
     LCLLSKLFLD HKTLYYDVDP FLFYCMTQRD ELGHHLVGYF SKEKESADGY NVACILTLPQ
     YQRMGYGRLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLIKL LVENGTEITI
     DEISSMTSLT TTDILHTAKA LNILRYYKGQ HILYLNEDVL LRYEKLIAKK RRSIDPEKLI
     WKPPIFTASQ LRFAW
//