ID   ESA1_CRYNB              Reviewed;         564 AA.
AC   P0CP03; Q55XW1; Q5KM33;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=CNBB2530;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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-381 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; AAEY01000009; EAL22621.1; -; Genomic_DNA.
DR   RefSeq; XP_777268.1; XM_772175.1.
DR   AlphaFoldDB; P0CP03; -.
DR   SMR; P0CP03; -.
DR   EnsemblFungi; AAW41586; AAW41586; CNB03160.
DR   GeneID; 4934345; -.
DR   KEGG; cnb:CNBB2530; -.
DR   VEuPathDB; FungiDB:CNBB2530; -.
DR   HOGENOM; CLU_011815_2_0_1; -.
DR   OrthoDB; 118560at2759; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..564
FT                   /note="Histone acetyltransferase ESA1"
FT                   /id="PRO_0000410158"
FT   DOMAIN          36..112
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          281..552
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         314..339
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           364..385
FT                   /note="ESA1-RPD3 motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        68..84
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..229
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        457
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         422..426
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         431..437
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         461
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   SITE            423
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   MOD_RES         381
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
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
//