GenomeNet

Database: UniProt
Entry: W1P3C7_AMBTC
LinkDB: W1P3C7_AMBTC
Original site: W1P3C7_AMBTC 
ID   W1P3C7_AMBTC            Unreviewed;       570 AA.
AC   W1P3C7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=AMTR_s00002p00268390 {ECO:0000313|EMBL:ERN01460.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN01460.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
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; KI394767; ERN01460.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1P3C7; -.
DR   STRING; 13333.W1P3C7; -.
DR   EnsemblPlants; ERN01460; ERN01460; AMTR_s00002p00268390.
DR   Gramene; ERN01460; ERN01460; AMTR_s00002p00268390.
DR   eggNOG; KOG1472; Eukaryota.
DR   HOGENOM; CLU_015741_5_0_1; -.
DR   OMA; FAQPVNR; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:UP000017836};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          228..375
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          473..544
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..136
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  64334 MW;  EB04F39B91E65EC4 CRC64;
     MDVHSGQSGG GGGVLSRSRA TSQSPSPSHS ASASVSATSA HPLTTSTTTH PNPNKRKLPS
     SPHHLPPPHP HPPSHPLSLS NDDLDSLSAR ADSDPVSLSN SEDRSEEEEE NSEEEEEENS
     EEEEEEMEDD EEDDDSMRTF TNARLSSKPK GEVGSSGIEK VSELGVKEER EKDRGSNQVA
     GSGLAVKDDS VKSVFTDNIQ TSGAYCARED SLKKEEDAGR LKFVCFANDG VDEHMIWLIG
     LKNIFARQLP NMPKEYIVRL VMDRSHKSVM IIKNNQVVGG ITYRPYVGQK FGEIAFCAIA
     TDEQVKGYGT RLMNHLKQHA RDVDGLTHFL TYADNNAVGY FIKQGFSKEI ELERERWQGY
     IKDYDGGILM ECKIDPKLPY TDLSAMIRQQ RQAIDEKIRE LSNCHIIYPG IDFQKKEAGI
     SRKKVEDIPG LREAGWTPDQ WGHTRFRAFS PAEIPNHRQQ LNSFMRSLHK VLSEHADAWP
     FKEPVDARDV PDYYDVIKDP MDLRTMSKRL ESEQYYVTFE MFVADVKRMF ANARTYNSPD
     TIYYKLANRL ESFFSNKVQA WLQASTKGQQ
//
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