GCN5_ASHGO
ID GCN5_ASHGO Reviewed; 452 AA.
AC Q756G9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=AER297C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). Acetylation of histones gives a
CC specific tag for epigenetic transcription activation (By similarity).
CC In addition to histone acetyltransferase, can use different acyl-CoA
CC substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and is able to
CC mediate histone crotonylation (By similarity).
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016818; AAS52978.1; -; Genomic_DNA.
DR RefSeq; NP_985154.1; NM_210508.1.
DR AlphaFoldDB; Q756G9; -.
DR SMR; Q756G9; -.
DR STRING; 33169.AAS52978; -.
DR EnsemblFungi; AAS52978; AAS52978; AGOS_AER297C.
DR GeneID; 4621367; -.
DR KEGG; ago:AGOS_AER297C; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_015741_2_0_1; -.
DR InParanoid; Q756G9; -.
DR OMA; RWMGYIK; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0140671; C:ADA complex; IEA:EnsemblFungi.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; 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:0046695; C:SLIK (SAGA-like) 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:0140068; F:histone crotonyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IEA:EnsemblFungi.
DR GO; GO:0003712; F:transcription coregulator activity; 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 GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; 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..452
FT /note="Histone acetyltransferase GCN5"
FT /id="PRO_0000211195"
FT DOMAIN 113..268
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 357..427
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 190..192
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 197..203
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 229..232
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT SITE 186
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 52414 MW; 9BA78D49039CAC66 CRC64;
MSMPLKRRNK QSQGNEPKKI KVEEQEAEEK ISEDIPVTDL KEPEALADIQ STSGGDEVSE
GAQGDADPAE KSVGGLKEEV EDEEKGIVKF MFDGVEYKFR ERPSVIEEKE GKIEFRVVNN
DNTRENMMVL TGLKNIFQKQ LPKMPKEYIA RLVYDRSHLS MAVIRKPLTV VGGITYRPFE
KGEFAEIVFC AISSTEQVRG YGAHLMNHLK DYVRATTNIK YFLTYADNYA IGYFKKQGFT
KEITLDKSVW MGYIKDYEGG TLMQCFMLPR IRYLDAAKIL LLQEAAIQRK IRTISRSHIV
RPGLRQFEDL DNIEPIDPMS VPGLREAGWT PEMDELAQRP KRGPHYATMQ NVLTELQNHA
AAWPFLQPVN RDEVPDYYEF IKEPMDLSTM EIKLENNRYE KMEDFIYDAR LIFNNCRAYN
GENTSYFKYA NRLEKFFNTK MKEIPEYSHL LD
