ID   GCN5_DEBHA              Reviewed;         455 AA.
AC   Q6BGW1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000305};
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q03330};
DE   AltName: Full=Histone crotonyltransferase GCN5 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q03330};
GN   Name=GCN5; OrderedLocusNames=DEHA2G23474g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Histone acetyltransferase that acetylates histone H2B to form
CC       H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower
CC       preference histone H4 to form H4K8ac and H4K16ac, and contributes to
CC       H2A.Z acetylation. Acetylation of histones gives a specific tag for
CC       epigenetic transcription activation. In addition to histone
CC       acetyltransferase, can use different acyl-CoA substrates, such as (2E)-
CC       butenoyl-CoA (crotonyl-CoA) and is able to mediate histone
CC       crotonylation. {ECO:0000250|UniProtKB:Q03330}.
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; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:Q03330};
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:Q03330};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR382139; CAG91071.2; -; Genomic_DNA.
DR   RefSeq; XP_462560.2; XM_462560.1.
DR   AlphaFoldDB; Q6BGW1; -.
DR   SMR; Q6BGW1; -.
DR   STRING; 284592.Q6BGW1; -.
DR   GeneID; 2905516; -.
DR   KEGG; dha:DEHA2G23474g; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   HOGENOM; CLU_015741_2_0_1; -.
DR   InParanoid; Q6BGW1; -.
DR   OMA; FAQPVNR; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR037800; GCN5.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR45750; GH11602P; 1.
DR   PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Activator; Acyltransferase; Bromodomain; Chromatin regulator; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..455
FT                   /note="Histone acetyltransferase GCN5"
FT                   /id="PRO_0000211197"
FT   DOMAIN          114..269
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   DOMAIN          359..429
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..82
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         191..193
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         198..204
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         230..233
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   SITE            187
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  52412 MW;  BB3B6869D316C09D CRC64;
     MVDRKRNSSV ISDNEENGRV DKKTKIKDEI EGDEVERDVK NEEANGADTD DKEEVRKDNE
     EENAENGGGE GDDDDDDDDE AEEEKKRTTT FNFDGVTYSF KERPSVLEEK EGKIEFRVVN
     NDNTKESLMV LTGLKNIFQK QLPKMPREYI SRLVYDRSHL SMAVVRKPLT VVGGITYRPF
     DNREFAEIVF CAISSTEQVR GYGAHLMNHL KDYCRATSNV KYFLTYADNY AIGYFKKQGF
     NKEITLDKSV WMGYIKDYEG GTLMQCSMLP PILRYLDSAK ILLLQKAAIE KKIKLRSKAH
     VVRPGLQVFK TNKDAKLNPA KDIPGLAESG WSEEMDKLAQ KPKRGPHYNF MVTLLSELTN
     HPSAWPFSTP VNKEEVGDYY DVIKEPMDLS TMESKLENDK YDSFDQFLYD ARLIFNNCRS
     YNADSTTYFK NATKLEKFMN NKIKDSAEYS HFLDQ
//