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Database: UniProt
Entry: A0A074YCQ0_AURSE
LinkDB: A0A074YCQ0_AURSE
Original site: A0A074YCQ0_AURSE 
ID   A0A074YCQ0_AURSE        Unreviewed;       427 AA.
AC   A0A074YCQ0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=AUEXF2481DRAFT_29003 {ECO:0000313|EMBL:KEQ95568.1};
OS   Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS   subglaciale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ95568.1, ECO:0000313|Proteomes:UP000030641};
RN   [1] {ECO:0000313|EMBL:KEQ95568.1, ECO:0000313|Proteomes:UP000030641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ95568.1,
RC   ECO:0000313|Proteomes:UP000030641};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584758; KEQ95568.1; -; Genomic_DNA.
DR   RefSeq; XP_013344116.1; XM_013488662.1.
DR   AlphaFoldDB; A0A074YCQ0; -.
DR   STRING; 1043005.A0A074YCQ0; -.
DR   GeneID; 25363843; -.
DR   HOGENOM; CLU_015741_1_1_1; -.
DR   InParanoid; A0A074YCQ0; -.
DR   OMA; FAQPVNR; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000030641; 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:UP000030641};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          77..232
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          324..394
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..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  48471 MW;  1F6EB707E2428969 CRC64;
     MAPAVIKEEG ATTNKRKAES PSESVGDSKR FKSSTSPTPT PTLPLAHDTG DAVQSTAPRV
     VPFPEKPAVI EERNGEIEFR AVNNDGDRES YIILTGLKCI FQKQLPKMPK DYIARLVYDR
     THLSMAIVKK PLEVVGGITY RPFKGRQFAE IVFCAISSDQ QVKGYGAHLM SHLKDYVKAT
     SDVMHFLTYA DNYAIGYFKK QGFTKEITLE RPRWMGYIKD YEGGTIMQCS MLPKIRYLES
     GRLLLKQKAA VHAKIKAVSK SFEVHPPPSQ WKGLKKGDNL PAIDPLTIGA IKETGWSLDM
     DALARQPRHN PNHSQLMHLL SALQNSTHAW PFLQPVNKDE VLDYYDVIKQ PMDLSTMEQK
     LENDAYETPE DFIRDATLIS VNCRRYNAEQ TPYHKAAIKL EKELWKKVKD VPEWSYIEQE
     HFAEVGK
//
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