ESA1_ASPOR
ID ESA1_ASPOR Reviewed; 506 AA.
AC Q2UMQ5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=AO090001000664;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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-318 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; AP007154; BAE57160.1; -; Genomic_DNA.
DR RefSeq; XP_001819162.1; XM_001819110.2.
DR AlphaFoldDB; Q2UMQ5; -.
DR SMR; Q2UMQ5; -.
DR STRING; 510516.Q2UMQ5; -.
DR EnsemblFungi; BAE57160; BAE57160; AO090001000664.
DR GeneID; 5991133; -.
DR KEGG; aor:AO090001000664; -.
DR VEuPathDB; FungiDB:AO090001000664; -.
DR HOGENOM; CLU_011815_2_0_1; -.
DR OMA; SMTQNQT; -.
DR Proteomes; UP000006564; 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: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; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..506
FT /note="Histone acetyltransferase ESA1"
FT /id="PRO_0000234078"
FT DOMAIN 27..80
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 218..494
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 251..276
FT /note="C2HC MYST-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 83..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 301..322
FT /note="ESA1-RPD3 motif"
FT COMPBIAS 83..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 359..363
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 368..374
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 398
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT SITE 360
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT MOD_RES 318
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
SQ SEQUENCE 506 AA; 58335 MW; B7FE46EDE0DA5846 CRC64;
MGVRDSHGEA TATPDPVEKG FATLNTIRIG VKAMVQKDGE LRKAEILSIR QRKDGPSFYV
HYVDFNKRLD EWIDSTRIDL SHEVEWPQPE KPEKKKAGPG NKAPSKNAQK RARAGSREVS
ATPDLLTGKN TNIGKAQRPS KAGGKENRDE TPANLSVLDS EAISADVTPK PEMEDVDMIG
VSFTDTKEEH EQGKMSREEE IERLRTSGSM TQNPTEIHRV RNLNRLQMGK FDIEPWYFSP
YPASFSDVDM VYIDEFCLSY FDNKRAFERH RSKCTLVHPP GNEIYRDDRI SFFEVDGRRQ
RTWCRNLCLL SKLFLDHKTL YYDVDPFLFY CMATRDETGC HLVGYFSKEK DSAEGYNLAC
ILTLPQYQRL GYGRLLIAFS YELSKREGKL GSPEKPLSDL GLLSYRQYWR ETLVELLIEP
GRESMSENEL AVLTSMTEKD VHETLVVFNM LRYHKGNWVI VLTDQVVEQH NKRLEKEKIK
GSRKIDPARL QWKPPVFTAS SRTWNW
