ID   ESA1_GIBZE              Reviewed;         502 AA.
AC   Q4IEV4; A0A0E0S6V1; V6R4L8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 118.
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; ORFNames=FGRRES_04254, FGSG_04254;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
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-316 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; DS231664; ESU08867.1; -; Genomic_DNA.
DR   EMBL; HG970333; CEF79226.1; -; Genomic_DNA.
DR   RefSeq; XP_011321366.1; XM_011323064.1.
DR   AlphaFoldDB; Q4IEV4; -.
DR   SMR; Q4IEV4; -.
DR   STRING; 229533.Q4IEV4; -.
DR   GeneID; 23551513; -.
DR   KEGG; fgr:FGSG_04254; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G14849; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_0_1; -.
DR   InParanoid; Q4IEV4; -.
DR   OrthoDB; 118560at2759; -.
DR   PHI-base; PHI:1637; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
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: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; 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; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..502
FT                   /note="Histone acetyltransferase ESA1"
FT                   /id="PRO_0000051557"
FT   DOMAIN          28..80
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          216..490
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         249..274
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           299..320
FT                   /note="ESA1-RPD3 motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        88..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        392
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         357..361
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         366..372
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   BINDING         396
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   SITE            358
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
FT   MOD_RES         316
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q08649"
SQ   SEQUENCE   502 AA;  58095 MW;  61DCF761F2C3CD43 CRC64;
     MAGGTPGGEP TVGSGEPRLK SLATPETIKT GCIAWVEKEG QPRRAEILSI KTTKSGKQFY
     CNFDNFNKRL DEWVPVIRLD FTREVEWPNP EKEKPKDPKA KKAPTVQSKK TQPSKKSQKR
     PSKREQSTTS EANTPHPWTD FVENQNRQKS ASIGPDGDSQ ARASVDGGET PGGGDEMEVD
     ERETEVKREP AEFSREVEIE KLRTSGSMTQ NPTEVSRIRN ISKVQFGRFD LYPWYFSPYP
     EIFSQEDVIF ICEFCLSYYG DLKAFTRHRK KCTLQHPPGN ELYRNEEISF FEIDGRRQRT
     WCRNLCLLSK MFLDHKTLYY DVDPFLFYVM TVRTEKGCHM VGYFSKEKES ADGYNVACIL
     TMPQYQRKGY GRLLIQFSYE LSRIEGKLGS PEKPLSDLGL LSYRQYWSEN ILEFLMGYNE
     RDEKVTIEAI STALAMTTQD VEHTLQALRM QVYHKSDHKI VIPEKLIEQR EKTKLKRKRT
     VDPTKIQWKP PVFTASSRTW GW
//