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Database: UniProt
Entry: I3J2D6_ORENI
LinkDB: I3J2D6_ORENI
Original site: I3J2D6_ORENI 
ID   I3J2D6_ORENI            Unreviewed;       792 AA.
AC   I3J2D6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|PIRNR:PIRNR003048};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|PIRNR:PIRNR003048};
GN   Name=LOC100700997 {ECO:0000313|Ensembl:ENSONIP00000003026.1};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000003026.1, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000003026.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR003048};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003048}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008607, ECO:0000256|PIRNR:PIRNR003048}.
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DR   RefSeq; XP_003444106.1; XM_003444058.2.
DR   AlphaFoldDB; I3J2D6; -.
DR   STRING; 8128.ENSONIP00000003026; -.
DR   Ensembl; ENSONIT00000003027.2; ENSONIP00000003026.1; ENSONIG00000002420.2.
DR   GeneID; 100700997; -.
DR   KEGG; onl:100700997; -.
DR   CTD; 8850; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   GeneTree; ENSGT00940000154995; -.
DR   HOGENOM; CLU_015901_0_0_1; -.
DR   OrthoDB; 1760108at2759; -.
DR   TreeFam; TF105399; -.
DR   Proteomes; UP000005207; Linkage group LG22.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043992; F:histone H3K9 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0060173; P:limb development; IEA:Ensembl.
DR   GO; GO:1903010; P:regulation of bone development; IEA:Ensembl.
DR   GO; GO:0061035; P:regulation of cartilage development; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR016376; GCN5/PCAF.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR009464; PCAF_N.
DR   PANTHER; PTHR45750; GH11602P; 1.
DR   PANTHER; PTHR45750:SF2; HISTONE ACETYLTRANSFERASE KAT2B; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF06466; PCAF_N; 1.
DR   PIRSF; PIRSF003048; Histone_acetylase_PCAF; 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   Acyltransferase {ECO:0000256|PIRNR:PIRNR003048};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR003048};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR003048};
KW   Transferase {ECO:0000256|PIRNR:PIRNR003048}.
FT   DOMAIN          465..613
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          700..770
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        532
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT   BINDING         536..538
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT   BINDING         543..549
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT   BINDING         574..577
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
SQ   SEQUENCE   792 AA;  89788 MW;  D934CBF374EEC118 CRC64;
     MADSAGIQQG SPAIGAAGLV PAAPGAGGTE GSGAARGSAR IAVKKAQLRS SPRPKKLEKL
     GVYSSCKAEG ACKCNGWKSQ NPPPTPPQTE QQSNAVNLQE PCRSCSHTLG DHVTHLENVS
     EEEMNRLLGI VLDVEYLYTC IHKEEDADTK QVYFSLFKLL RKSILQMGKP MLEAQESPPF
     EKPSIEQGVN NFVQYKFSHL PSKERQTIME LAKMFLNQIN YWQLETPSQR RQRVPNDDAA
     GYKVNYTRWL CYCNVPQFCD SLPRYETTQI FGRTLLRSVF TVMRKQLLEQ ARQEKDKLPP
     EKRTLILTHF PKFLSMLEEE VYSHNSPIWS QDFLAGAAGG QIPIHTVISA ASVARPLYYS
     TSPVSVDPST CGSVSPARKA ASVLEPNPAG EKRKPSEPLP HEENKRPRVV GDIPMDLINE
     VMATITDPAA IPETSLLSAH SARDEAARLE ERRGVIEFHV IGNSLNQKPN KRILMWLVGL
     QNVFSHQLPR MPKEYITRLV FDPKHKTLSL IKDGRVIGGI CFRMFPSQGF TEIVFCAVTS
     NEQVKGYGTH LMNHLKEYHI KHEILNFLTY ADEYAIGYFK KQGFSKDIKV PKSKYVGYIK
     DYEGATLMGC ELNPSIPYTE FSVIIKKQKE IIKKLIERKQ AQIRKVYPGL SCFKDGVRQI
     PIESIPGIRE TGWKPVGKGK ELKDPDQLYS TLKTILQHVK SHQNAWPFME PVKKTEAPGY
     YQVIRFPMDL KTMSERLKSR YYTTRKLFMA DMQRIFTNCR EYNPPESEYY KCANLLEKFF
     YTKIKEAGLI EK
//
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