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Database: UniProt
Entry: A0A179UFD7_BLAGS
LinkDB: A0A179UFD7_BLAGS
Original site: A0A179UFD7_BLAGS 
ID   A0A179UFD7_BLAGS        Unreviewed;       402 AA.
AC   A0A179UFD7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=BDBG_02277 {ECO:0000313|EMBL:OAT05979.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT05979.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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:0000256|ARBA:ARBA00000780};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008607}.
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DR   EMBL; GG657450; OAT05979.1; -; Genomic_DNA.
DR   RefSeq; XP_002627606.1; XM_002627560.1.
DR   AlphaFoldDB; A0A179UFD7; -.
DR   STRING; 559298.A0A179UFD7; -.
DR   GeneID; 8510252; -.
DR   KEGG; bgh:BDBG_02277; -.
DR   VEuPathDB; FungiDB:BDBG_02277; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; GH11602P; 1.
DR   PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF47370; Bromodomain; 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 {ECO:0000256|ARBA:ARBA00023159};
KW   Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          65..220
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          307..377
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  46519 MW;  418EB80637F2A066 CRC64;
     MAPIALDRGK RKASEEYAEG DDTVHRVKRA RTESPKEDQE DDKQVLKLVP YPEKPAVIEE
     RKGEIEFRVV NNDGERESFI ILTGLKCIFQ KQLPKMPKDY IARLVYDRTH LSIAIVKQPL
     EVVGGITFRP FKGRKFAEIV FCAISSDQQV KGYGAHLMSH LKDYVKATSD VMHFLTYADN
     YALGYFKKQG FTKEITLEKS VWMGYIKDYE GGTIMQCTML PKIRYLEAGR MLLKQKAAVH
     AKIRAFSKSH IVHAPPKEWK NGAFKIDPLS VPAIKESGWS PDMDELARQP RHGPNYNQLL
     HLLNDMQNHS SAWPFVQPVN RDEVPDYYEV IQEPMDLSTM EEKHEKDMYP TPEDFIKDAN
     LIFDNCRKYN NENTAYVKSA NKLEKFMWQQ IKNVPEWSHL AD
//
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