ESA1_ASHGO
ID ESA1_ASHGO Reviewed; 435 AA.
AC Q75BY2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 121.
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 Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016816; AAS51364.2; -; Genomic_DNA.
DR RefSeq; NP_983540.2; NM_208893.2.
DR AlphaFoldDB; Q75BY2; -.
DR SMR; Q75BY2; -.
DR STRING; 33169.AAS51364; -.
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; SMTQNQT; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0000786; C:nucleosome; IEA:EnsemblFungi.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0140068; F:histone crotonyltransferase activity; IEA:EnsemblFungi.
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 transcription, DNA-templated; 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 from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:EnsemblFungi.
DR Gene3D; 1.10.10.10; -; 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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 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
