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Database: UniProt
Entry: A0A3Q1BZQ5_AMPOC
LinkDB: A0A3Q1BZQ5_AMPOC
Original site: A0A3Q1BZQ5_AMPOC 
ID   A0A3Q1BZQ5_AMPOC        Unreviewed;       792 AA.
AC   A0A3Q1BZQ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
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};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000019830.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000019830.1}
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   AlphaFoldDB; A0A3Q1BZQ5; -.
DR   STRING; 80972.ENSAOCP00000019830; -.
DR   Ensembl; ENSAOCT00000014623.1; ENSAOCP00000019830.1; ENSAOCG00000003484.1.
DR   GeneTree; ENSGT00940000154995; -.
DR   OMA; DFAIGYF; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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:UP000257160};
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..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..404
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;  89728 MW;  56F004B7DBE87F6D CRC64;
     MADSGGIQQG SPAIGAAGLV PAAPGAGGTE GSGAAGGSAR IAVKKAQLRS SPRPKKLEKL
     GVYSSCKAEG ACKCNGWKSQ NPPPTPPQTD QQSNAVNLQE PCRSCSHTLG DHVTHLENVS
     EEEMNRLLGI VLDVEYLYTC VHKEEDADTK QVYFSLFKLL RKSILQMGKP MLEAQESPPF
     EKPSIEQGVN NFVQYKFSHL PSKERQTIME LAKMFLNQIN YWQLETPSQR RQRVPNDDAA
     GYKANYTRWL CYCNVPQFCD SLPRYETTQI FGRTLLRSVF TVMRKQLLEQ ARQEKDKLPP
     EKRTLILTHF PKFLSMLEEE VYSHSSPIWS QDFLAGAAGG QIPIHTVISA PPVARPLYYS
     TSPVSVDPST CGSVSPARKT ASVLETNPVG EKRKPTEPLH HEENKRPRVV GDIPMDLINE
     VMATITDPAA IPETSLLSAH SARDEAARLE ERRGVIEFHV IGNSLNQKPN KRILMWLVGL
     QNVFSHQLPR MPKEYITRLV FDPKHKTLSL IKDGRVIGGI CFRMFPSQGF TEIVFCAVTS
     NEQVKGYGTH LMNHLKEYHI KHEILNFLTY ADEYAIGYFK KQGFSKDIKV PKAKYVGYIK
     DYEGATLMGC ELNPSIPYTE FSVIIKKQKE IIKKLIERKQ AQIRKVYPGL SCFKDGVRQI
     PIESIPGIRE TGWKPVGKGK ELKDPDQLYS TLKTILQHVK SHQNAWPFME PVKKTEAPGY
     YQVIRFPMDL KTMSERLKSR YYTTRKLFMA DMQRIFTNCR EYNPPESEYY KCANLLEKFF
     YTKIKEAGLI EK
//
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