GCN5_KLULA
ID GCN5_KLULA Reviewed; 516 AA.
AC Q6CXW4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=KLLA0A05115g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382121; CAH02813.1; -; Genomic_DNA.
DR RefSeq; XP_451225.1; XM_451225.1.
DR AlphaFoldDB; Q6CXW4; -.
DR SMR; Q6CXW4; -.
DR STRING; 28985.XP_451225.1; -.
DR PRIDE; Q6CXW4; -.
DR EnsemblFungi; CAH02813; CAH02813; KLLA0_A05115g.
DR GeneID; 2896739; -.
DR KEGG; kla:KLLA0_A05115g; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_015741_5_0_1; -.
DR InParanoid; Q6CXW4; -.
DR OMA; RWMGYIK; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000124; C:SAGA complex; IEA:EnsemblFungi.
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:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
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:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
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..516
FT /note="Histone acetyltransferase GCN5"
FT /id="PRO_0000211198"
FT DOMAIN 177..332
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 421..491
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 254..256
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 261..267
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 293..296
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT SITE 250
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ 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
