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Histone acetyltransferase GCN5 (EC 2.3.1.48)

 GCN5_KLULA              Reviewed;         516 AA.
Q6CXW4;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
20-JUN-2018, entry version 92.
RecName: Full=Histone acetyltransferase GCN5;
EC=2.3.1.48;
Name=GCN5; OrderedLocusNames=KLLA0A05115g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Acetylates histone H2B to form H2BK11ac and H2BK16ac,
histone H3 to form H3K14ac, with a lower preference histone H4 to
form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation.
Acetylation of histones gives a specific tag for epigenetic
transcription activation (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
subfamily. {ECO:0000305}.
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EMBL; CR382121; CAH02813.1; -; Genomic_DNA.
RefSeq; XP_451225.1; XM_451225.1.
ProteinModelPortal; Q6CXW4; -.
STRING; 284590.XP_451225.1; -.
PRIDE; Q6CXW4; -.
EnsemblFungi; CAH02813; CAH02813; KLLA0_A05115g.
GeneID; 2896739; -.
KEGG; kla:KLLA0A05115g; -.
eggNOG; KOG1472; Eukaryota.
eggNOG; COG5076; LUCA.
HOGENOM; HOG000192257; -.
InParanoid; Q6CXW4; -.
KO; K06062; -.
OMA; GTIMQCS; -.
OrthoDB; EOG092C0SVC; -.
Proteomes; UP000000598; Chromosome A.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IEA:EnsemblFungi.
GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblFungi.
GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
GO; GO:0000124; C:SAGA complex; IEA:EnsemblFungi.
GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:EnsemblFungi.
GO; GO:0010484; F:H3 histone acetyltransferase activity; IEA:EnsemblFungi.
GO; GO:0070577; F:lysine-acetylated histone binding; IEA:EnsemblFungi.
GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR037800; GCN5.
InterPro; IPR000182; GNAT_dom.
PANTHER; PTHR22880:SF124; PTHR22880:SF124; 1.
Pfam; PF00583; Acetyltransf_1; 1.
Pfam; PF00439; Bromodomain; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51186; GNAT; 1.
3: Inferred from homology;
Activator; Acyltransferase; Bromodomain; Chromatin regulator;
Complete proteome; Nucleus; Reference proteome; Transcription;
Transcription regulation; Transferase.
CHAIN 1 516 Histone acetyltransferase GCN5.
/FTId=PRO_0000211198.
DOMAIN 177 332 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
DOMAIN 421 491 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
REGION 254 256 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 261 267 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 293 296 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
ACT_SITE 250 250 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q92830}.
SITE 250 250 Important for catalytic activity.
{ECO:0000250}.
SEQUENCE 516 AA; 59291 MW; F11C13FA976421F0 CRC64;
MPPKRRHHGA GRVQNKRGKV DTVKEEIKPK DEPVETEIDG GSAVDEDVTD DLEHKTSKED
QKEDQKEEDG PIDAQNGTSE TKVAGESVKT VEDKIESVTT NEEVVESPVN DYNASSTTTK
AEEKQLEEEA NEKTDTSPIV ENEVVDEEAG TTKFDFDGQE YSYKDRPSVI EEKEGKIEFR
VVNNDNSKEN MMVLTGLKNI FQKQLPKMPK EYIARLVYDR SHLSMAVVRK PLTVVGGITY
RPFDKREFAE IVFCAISSTE QVRGYGAHLM NHLKDYVRAT SPIKYFLTYA DNYAIGYFKK
QGFTKEITLD KNVWMGYIKD YEGGTLMQCS MLPRIRYLDA AKILLLQEAA IRRKIRSISQ
SHIVRPGLKQ FLDLDNIKPI DPMTIPGLKE AGWTPEMDEL AQRPKRGPHY AAMQNLLTEL
QNHAAAWPFL QPVNKEEVPD YYEFIKEPMD LSSMEMKLNG NRYEKMENFI YDARLIFNNC
RAYNGENTSY FKYANRLEKF FNSKVKEIPE YSHLVD


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