ID A0A3Q1CQ69_AMPOC Unreviewed; 794 AA.
AC A0A3Q1CQ69;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:ENSAOCP00000027604.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000027604.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3Q1CQ69; -.
DR STRING; 80972.ENSAOCP00000027604; -.
DR Ensembl; ENSAOCT00000030549.1; ENSAOCP00000027604.1; ENSAOCG00000016687.1.
DR GeneTree; ENSGT00940000158799; -.
DR OMA; ERYFQTK; -.
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:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-UniRule.
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:SF1; HISTONE ACETYLTRANSFERASE KAT2A; 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|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 460..613
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 702..772
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..50
FT /note="Polar 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 794 AA; 90641 MW; C976053DA47CAFAB CRC64;
MSDPAAQALQ PRLLQAQSAG SSTATTGSGS GNSDPSRPGL SQQQRASQKK AQVRAFPRAK
KLEKLGVFSA CKASDTCKCN GWKNPNPPSA TRMDLQQQAA SLSEPCRSCG HALADHVSHL
ENVSEEEINR LLGMVVDVEN LFMSVHKEED TDTKQVYFYL FKLLRKCILQ MSQPVVEGSL
GSPPFEKPNI EQGVLNFVQY KFSHLAPKER QTMFELSKMF LLCLNYWKLE TPTQYRQRTQ
KDDGTAYKVD YTRWLCYCHV PQSNDSLPRY ETTHVFGRNL LKSIFTVTRR QLLEKFRVEK
DKLLPEKRTL ILTHFPKFLS MLEEEIYGEN SPIWEADFTM PASDGTQLGH QTVISPPSVS
GSPALSKCLS SSSSLGSIDA GGVEPITGEK RKLPEVLTLE DAKRIRVMGD IPMELVNEVM
MTITDPAAML GPETNLLTPN AARDETARLE ERRGIIEFHV IGNSLSQKSN KKILMWLVGL
QNVFSHQLPR MPKEYITRLV FDPKHKTLAL IKDGRVIGGI CFRMFPTQGF TEIVFCAVTS
NEQVKGYGTH LMNHLKEYHI KHNILYFLTY ADEYAIGYFK KQGFSKDIKV PKSRYLGYIK
DYEGATLMEC ELNPRIPYTE LSHIIKRQKE IIKKLIERKQ SQIRKVYPGL TCFKEGVRQI
PVESIPGIRE TGWKPSNKDK GKEVKDPDVL YNMLKNLLAQ IKTHPDAWPF MEPVKKSEAP
DYYEIIRFPI DLKTMTERLK NRYYVTKKLF IADLQRIITN CREYNPPDSE YCKSANTLEK
FFYFKLKDGG LIEK
//