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Database: UniProt
Entry: A0A1Y2APY6_9TREE
LinkDB: A0A1Y2APY6_9TREE
Original site: A0A1Y2APY6_9TREE 
ID   A0A1Y2APY6_9TREE        Unreviewed;       551 AA.
AC   A0A1Y2APY6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=BCR39DRAFT_320510 {ECO:0000313|EMBL:ORY24592.1};
OS   Naematelia encephala.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Naemateliaceae; Naematelia.
OX   NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY24592.1, ECO:0000313|Proteomes:UP000193986};
RN   [1] {ECO:0000313|EMBL:ORY24592.1, ECO:0000313|Proteomes:UP000193986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-887.2 {ECO:0000313|EMBL:ORY24592.1,
RC   ECO:0000313|Proteomes:UP000193986};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107}.
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:ORY24592.1}.
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DR   EMBL; MCFC01000066; ORY24592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2APY6; -.
DR   STRING; 71784.A0A1Y2APY6; -.
DR   InParanoid; A0A1Y2APY6; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000193986; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF180; HISTONE ACETYLTRANSFERASE SAS2; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Acyltransferase {ECO:0000313|EMBL:ORY24592.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193986};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ORY24592.1}.
FT   DOMAIN          121..501
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          100..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        369
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   551 AA;  61814 MW;  9D14D4AB51A616D0 CRC64;
     MMSDPARSSQ ATVKQEQAGT KWVIGAQYLV ARPGAPPRVA VLQNVRTSRT NETEVYVNFL
     GEDKRLDSWL GEECVVGIGS NGEGSSKRRK VNDGLVSFID GRSEGSSSAA STPEREHEAM
     TRVRNFEDVR FGEYLIKTWY YSPYPMPMDD LPTTTSTTPK VNGDSGSKKR KSLQGSVSTI
     SSNGESNHHT EGLGRKARSV PEMLASGVGK GAERARGRLW ACDLCFKYMR TRAAWDRHCA
     TCDMLLPPGR RVYQRGSYTI WEVDGSQAPL YCQNLSLFGK LFIDHKSVFF HVENFLFYVL
     CDASTSRRDQ VMAFFSKEKL SYDDYNLACI VTFPPFQNRG FGKLLIEFSY YLTKHPSTRL
     PSKSPGTPER PLSDLGLKGY TTYWMSVVLR VLHGLLKDTV PLDIVAATPK KEGRSMRVRA
     RHGQTEPEII RIEGIEVYKT PDVAYTGQYS VHLSLALLAK ACHLRTDDVA FTLTELGFLI
     HRRDLSTTEI AGSARLFEAP PDPEIKEISA AGEQGEWAGV EVVVDRGMVE EQWKLWRVRE
     KGVLDEQYIL L
//
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