GCN5_YARLI
ID GCN5_YARLI Reviewed; 464 AA.
AC Q8WZM0; Q6C789;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Histone acetyltransferase GCN5;
DE EC=2.3.1.48;
GN Name=GCN5; OrderedLocusNames=YALI0E02772g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=INAG 35668;
RA Gonzalez-Prieto J., Dominguez-Olavarri A., Ruiz-Herrera J.;
RT "Isolation and characterization of the GCN5 gene of Yarrowia lipolytica.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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: Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone
CC H3 to form H3K14ac, with a lower preference histone H4 to form H4K8ac
CC and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of
CC histones gives a specific tag for epigenetic transcription activation
CC (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ237940; CAC80210.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG79052.1; -; Genomic_DNA.
DR RefSeq; XP_503473.1; XM_503473.1.
DR AlphaFoldDB; Q8WZM0; -.
DR SMR; Q8WZM0; -.
DR STRING; 4952.CAG79052; -.
DR EnsemblFungi; CAG79052; CAG79052; YALI0_E02772g.
DR GeneID; 2912645; -.
DR KEGG; yli:YALI0E02772g; -.
DR VEuPathDB; FungiDB:YALI0_E02772g; -.
DR HOGENOM; CLU_015741_2_0_1; -.
DR InParanoid; Q8WZM0; -.
DR OMA; RWMGYIK; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IEA:EnsemblFungi.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0036408; F:histone acetyltransferase activity (H3-K14 specific); IEA:EnsemblFungi.
DR GO; GO:0043993; F:histone acetyltransferase activity (H3-K18 specific); IEA:EnsemblFungi.
DR GO; GO:0043992; F:histone acetyltransferase activity (H3-K9 specific); IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:1905533; P:negative regulation of leucine import across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..464
FT /note="Histone acetyltransferase GCN5"
FT /id="PRO_0000211200"
FT DOMAIN 127..282
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 369..439
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 204..206
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 211..217
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 243..246
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT SITE 200
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 54096 MW; A7F3FC0C3B6D2CC4 CRC64;
MDSDTESVKR RKSSGSESES SVRDPKRTKI EDEDFQENGI DDEDEEEEEE EAKDEGDEDD
EEKGEDDEED DEEKEGEDGE GEEEDEEEDE EKKREEEEKY VTSFNFDGVE YKYKERPAVI
EEREGKIEFR VVNNDNSKEN LMILTGLKNI FQKQLPKMPR EYIARLVYDR SHVSMAVVRK
PLTVVGGITF RPFDTRKFAE IVFCAISSTE QVRGYGAHLM NHLKDYVKAT SPVMYFLTYA
DNYAIGYFKK QGFSKEISLD RSVWMGYIKD YEGGTLMQCS MLPRIRYLDV NKILLLQKAL
IHKKIRAISK SHVVRKGLDH FRDSTTPVDP MTIPGLKEAG WTPEMDELAR RPKRGPHFAV
MQHVLSELQN HASAWPFAQA VNRDEVPDYY EVIKEPMDLS TMEQRLEADS YKTMEEFVYD
ARLVFNNCRA YNNETTTYYK NANKLEKFMV AKIKEIPEYS HLVE
