GCN5_DEBHA
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 03-AUG-2022, entry version 104.
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 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; 4959.XP_462560.2; -.
DR EnsemblFungi; CAG91071; CAG91071; DEHA2G23474g.
DR GeneID; 2905516; -.
DR KEGG; dha:DEHA2G23474g; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_015741_2_0_1; -.
DR InParanoid; Q6BGW1; -.
DR OMA; RWMGYIK; -.
DR OrthoDB; 349249at2759; -.
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 GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 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; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 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
