ESA1_CRYNB
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 03-AUG-2022, entry version 57.
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 EnsemblFungi; EAL22621; EAL22621; CNBB2530.
DR GeneID; 4934345; -.
DR KEGG; cnb:CNBB2530; -.
DR VEuPathDB; FungiDB:CNBB2530; -.
DR HOGENOM; CLU_011815_2_0_1; -.
DR Proteomes; UP000001435; Chromosome 2.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
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 acetyltransferase activity (H3-K4 specific); 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:0034508; P:centromere complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR GO; GO:0031452; P:negative regulation of heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0048478; P:replication fork protection; IEA:EnsemblFungi.
DR Gene3D; 1.10.10.10; -; 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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 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; 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
