GCN5_CANGA
ID GCN5_CANGA Reviewed; 546 AA.
AC Q6FTW5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=CAGL0F08283g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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; CR380952; CAG59253.1; -; Genomic_DNA.
DR RefSeq; XP_446329.1; XM_446329.1.
DR AlphaFoldDB; Q6FTW5; -.
DR SMR; Q6FTW5; -.
DR STRING; 5478.XP_446329.1; -.
DR PRIDE; Q6FTW5; -.
DR EnsemblFungi; CAG59253; CAG59253; CAGL0F08283g.
DR GeneID; 2887572; -.
DR KEGG; cgr:CAGL0F08283g; -.
DR CGD; CAL0131206; GCN5.
DR VEuPathDB; FungiDB:CAGL0F08283g; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_015741_2_0_1; -.
DR InParanoid; Q6FTW5; -.
DR OMA; MKLEARE; -.
DR Proteomes; UP000002428; Chromosome F.
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:0000124; C:SAGA complex; IEA:EnsemblFungi.
DR GO; GO:0046695; C:SLIK (SAGA-like) 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: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; 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: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..546
FT /note="Histone acetyltransferase GCN5"
FT /id="PRO_0000211196"
FT DOMAIN 207..362
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 451..521
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 284..286
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 291..297
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 323..326
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT SITE 280
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 546 AA; 63512 MW; 977FDACF889D0189 CRC64;
MVTRRRLHHP EVEQVSKRQK VDKAESKNKK HADVAAERGE QSTEDHEDES QDKKDKKVVG
DNRDEDEEVS PNGQEAAEDN DDRKDKDAKE KDTETNDEGT EKSHTDVNDD DDDVDESKEE
DAAAAVDITK EKKDEQESDN KTEEKKVQEN EEEEEEDENK NDEDVEELGS TEPVDDEKKG
LVKFEFDGVE YKFKERASVI EENEGKIEFR VVSNDNTREN MMVLTGLKNI FQKQLPKMPK
EYIARLVYDR SHLSMAVIRK PLTVVGGITY KPFNKRQFAE IVFCAISSTE QVRGYGAHLM
NHLKDYVRNT SDIRYFLTYA DNYAIGYFKK QGFTKDITLD KKVWMGYIKD YEGGTLMQCS
MLPRIRYLDA AKILLLQEAA LRRKIRTISK SHVVHPGLEC FNDIENIKPI DPMSIPGLKE
AGWTPEMDEL AQRPKRGPHY AAIQNILVEL QNHAAAWPFL RPVNKEEVPD YYEFIKEPMD
LSTMELKLEN NKYEKMEEFI YDARLVCNNC RLYNGENTSY YKYANRLEKF FNNKVKEIPE
YSHLID
