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   27-MAR-2024, entry version 119.
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=KLLA0F11209g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
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-256 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; CR382126; CAG98298.1; -; Genomic_DNA.
DR   RefSeq; XP_455590.1; XM_455590.1.
DR   AlphaFoldDB; Q6CKE9; -.
DR   SMR; Q6CKE9; -.
DR   STRING; 284590.Q6CKE9; -.
DR   PaxDb; 284590-Q6CKE9; -.
DR   GeneID; 2895129; -.
DR   KEGG; kla:KLLA0_F11209g; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_0_1; -.
DR   InParanoid; Q6CKE9; -.
DR   OMA; QYQRHGY; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR   GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 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..439
FT                   /note="Histone acetyltransferase ESA1"
FT                   /id="PRO_0000051558"
FT   DOMAIN          23..73
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          156..427
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         189..214
FT                   /note="C2HC MYST-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          83..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           239..260
FT                   /note="ESA1-RPD3 motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        83..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         297..301
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         306..312
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         336
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   SITE            298
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   MOD_RES         256
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
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
//