ESA1_EMENI
ID ESA1_EMENI Reviewed; 508 AA.
AC C8VBH4; Q5AW35;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=AN10956;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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-320 is required for proper function.
CC {ECO:0000250|UniProtKB:Q08649}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA62075.1; Type=Erroneous gene model prediction; Note=The predicted gene AN7495 has been split into 2 genes: AN10944 and AN10956.; Evidence={ECO:0000305};
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DR EMBL; AACD01000129; EAA62075.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001304; CBF79494.1; -; Genomic_DNA.
DR RefSeq; XP_680764.1; XM_675672.1.
DR AlphaFoldDB; C8VBH4; -.
DR SMR; C8VBH4; -.
DR STRING; 162425.CADANIAP00000591; -.
DR PRIDE; C8VBH4; -.
DR EnsemblFungi; CBF79494; CBF79494; ANIA_10956.
DR EnsemblFungi; EAA62075; EAA62075; AN7495.2.
DR GeneID; 2869457; -.
DR KEGG; ani:AN7495.2; -.
DR VEuPathDB; FungiDB:AN10956; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_005700_0_0_1; -.
DR InParanoid; C8VBH4; -.
DR OMA; SMTQNQT; -.
DR OrthoDB; 629545at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0016573; P:histone acetylation; IMP:AspGD.
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 GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
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..508
FT /note="Histone acetyltransferase esa1"
FT /id="PRO_0000413170"
FT DOMAIN 27..80
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 220..496
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 253..278
FT /note="C2HC MYST-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 84..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 303..324
FT /note="ESA1-RPD3 motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 84..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 361..365
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 370..376
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 400
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT SITE 362
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT MOD_RES 320
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
SQ SEQUENCE 508 AA; 58152 MW; 148B5CA949A47101 CRC64;
MGVRDSHGEA AGTPDPVEKG IATLNTIRIG VKAMVHKDGA LRKAEILSIK QRKDGLAFYV
HYVDFNKRLD EWVASSRLDL SQEVEWPQPE KPEKKKSGPA KAPSKNKRVR AGSRDVSATP
DTLTGKNTNV GKAQRPSKAG GKENRGDETP ADLSMLASEA VSADGTPKAV SEDIDMMDAS
FTDAKEIKEE ERALGLMSRE EEIEKLRTSG SMTQNPTEVH RVRNLDRLQM GKYDIEPWYF
SPYPASFSDA EVVYIDEFCL SYFDNKRAFE RHRTKCTLTH PPGNEIYRDD NISFFEVDGR
RQRTWCRNLC LLSKLFLDHK TLYYDVDPFL FYCMCTRDET GCHLVGYFSK EKESGEGYNL
ACILTLPQYQ RRGYGRLLIS FSYELSKREG KVGSPEKPLS DLGLLGYRQY WRETLVEILL
DSGRETVSEN ELAMLTSMTE KDVHETLVTF KMLRYNKGQW IIVLTDEVIE ERNKRLEKEK
IKGSRKIDPA RLQWKPPVFT ASSRTWNW
