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Database: UniProt
Entry: A0A175WDS5_9PEZI
LinkDB: A0A175WDS5_9PEZI
Original site: A0A175WDS5_9PEZI 
ID   A0A175WDS5_9PEZI        Unreviewed;       403 AA.
AC   A0A175WDS5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=MMYC01_202985 {ECO:0000313|EMBL:KXX81815.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX81815.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX81815.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXX81815.1}.
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DR   EMBL; LCTW02000027; KXX81815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175WDS5; -.
DR   STRING; 100816.A0A175WDS5; -.
DR   VEuPathDB; FungiDB:MMYC01_202985; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000078237; 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:UP000078237};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:KXX81815.1}.
FT   DOMAIN          61..216
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..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  46237 MW;  3ECEE8E9577FDCC9 CRC64;
     MDKTESHSSP ADHNQNPVVK RAASEESNSA SGVKRIKHSH DAQPPALTLR PAVLEERNGE
     IEFRVVNNDG ARVSMVILTG LKCLFQKQLP KMPKDYIARL VYDRTHLSIA IVKTPLEVIG
     GITFREFRHR RFAEVVFCAV SSDQQVKGYG AHLMAHLKDY VKATSPVMHF LTYADNYATG
     YFQKQGFTKE ITLDRSVWMG YIKDYEGGTL MQCSMVPRIR YLEAGRMLLK QRETVLAKIR
     SLSRSHVVHQ PPRAWARHGA GAVTPVDPLS LPAIHATGWS PDMDELARVP RRGPHFNELR
     RFLYQIQNHK QAWPFLNPVN RDEVPDYYNV ITSPMDLSTM EERLERDCYA TPKDLVADLK
     LVFSNCRQYN DATTVYAKCA VKLEKYMWSL IREIPEWYEL VEE
//
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