ID A0A0P7BGC4_9HYPO Unreviewed; 1055 AA.
AC A0A0P7BGC4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Histone acetyltransferase ESA1 {ECO:0000313|EMBL:KPM40075.1};
GN ORFNames=AK830_g6490 {ECO:0000313|EMBL:KPM40075.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM40075.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM40075.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM40075.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00029286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000256|ARBA:ARBA00029286};
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:0000256|ARBA:ARBA00029298};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000256|ARBA:ARBA00029298};
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:0000256|ARBA:ARBA00024456};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000256|ARBA:ARBA00024456};
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:0000256|ARBA:ARBA00029280};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000256|ARBA:ARBA00029280};
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000256|ARBA:ARBA00011353}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM40075.1}.
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DR EMBL; LKCW01000091; KPM40075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BGC4; -.
DR STRING; 78410.A0A0P7BGC4; -.
DR OrthoDB; 5486876at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.50.10.10; -; 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 InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR008313; GH125.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR31047; MEIOTICALLY UP-REGULATED GENE 157 PROTEIN; 1.
DR PANTHER; PTHR31047:SF0; MEIOTICALLY UP-REGULATED GENE 157 PROTEIN; 1.
DR Pfam; PF06824; Glyco_hydro_125; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM01149; DUF1237; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KPM40075.1}.
FT DOMAIN 220..517
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1055 AA; 118218 MW; EFA7A3C87693D2B3 CRC64;
MAGGTPGAEP TVGSDGPRRK EKATPETLQT GCIAWVEKEG QPRRAEILSI KTTKSGMQFY
CNFDNFNKRL DEWVPAARID FSRDVEWPNP EKDKPKESKT KKAPSAAQSK KNQVSKKAQK
RPSKREQSVA SEANTPHPWT VVAEFVDSQT RQKSTSVGPE GESQTRPSVE GGATPATGED
MDADDKEEDV KKEQHDFSRE VEIEKLRTSG SMTQNPTEVS RIRNISKVQF GKNDLYPWYF
SPYPESFSQE DVIFLCEFCL GYYGDEKSFS RHRRKCTLQH PPGNEIYRDG LISFFEIDGR
RQRTWCRNLC LLSKMFLDHK TLYYDVDPFL FYVMTTRTEK GCHVVGYFSK EKESADGYNV
ACILTLPQYQ RKGYGRLLIQ FSYELSRIEG KLGSPEKPLS DLGLLSYRHD LNGVGHDNTG
RGAHAPGNED AGVPQERPQD CDTRQADQAA REGETEAEED GGRDQDPVEA AGVYGVKPNM
GLVRMVRDVT TLVGSDTLFQ LSSKQESDPN TVVAMTLRVL ASSLLGLGAQ LASASSDAQA
PVSDWSGACP EYTLYSTFPH RPFSSGPREL PFQRPKPQCR TFKSDEIERV IEEMTARIQD
PDLARLFENT FPSTTDTTVK FHTKGKEETG FFKMAGFGFR DEGAWEGPQS FIITGDIIAE
WLRDSTNQLR PYQPLAKKDP AIRTLLLGAI NTQAEYVIKS PYCNAFQPPP ISDLPVSNNG
QDDAVHPAYE PGVVFECKYE LDSLGHFLAL ANDFYDHVES TEFLNKRWYL AIDTLLQVLE
QQSKPTFDPE TGRYQRNEYT FQRHTNIGTE TLNLQGVGNP LNFGTGLVRS AFRPSDDATI
LGFFIPANAM MSVELQRTAT MLKAAGKASL AKTLEQWSKQ LRDGVLEHGI VKHKKYGDVF
AYEVDGYGSS ILMDDANYPS LLALPLMGFC ESSDPVYQNT RKMLLEKSGN PYYLTGRDFK
GIGGPHIGLR NAWPMSLLIQ AQTSDDDAEI KECLELVLDS AKLGLVHESI DVQYMSQYTR
SWFAWANGVF AVTMLDLAKR KPYLIFGEGA EPYAV
//
