ID A0A3Q3XF03_MOLML Unreviewed; 797 AA.
AC A0A3Q3XF03;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-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 Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000027275.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000027275.1}
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; A0A3Q3XF03; -.
DR STRING; 94237.ENSMMOP00000027275; -.
DR Ensembl; ENSMMOT00000027738.1; ENSMMOP00000027275.1; ENSMMOG00000020622.1.
DR OMA; YFQTKMR; -.
DR Proteomes; UP000261620; 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|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003048};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
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 463..616
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 705..775
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 535
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT BINDING 539..541
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 546..552
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 577..580
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
SQ SEQUENCE 797 AA; 90832 MW; 160C4000306FE820 CRC64;
MSDPAAQALQ PRLLQAQSGG SAGSSTATTG SGSGNSDPAR PGLNQQQRAS QKKAQVRAFP
RAKKLEKLGV FSACKAIDTC KCNGWKNPNP PSAPRMDLQQ QAASLSEPCR SCGHALADHV
SHLENVSEDE INRLLGMVVD VENLFMSVHK EEDTDTKQVY FYLFKLLRKC ILQMSQPVVE
GSLGSPPFEK PNIEQGVLNF VQYKFSHLAP KERQTMFELS KMFLLCLNYW KLETPTQYRQ
RTQKDDGTAY KVDYTRWLCY CHVPQSNDSL PRYETTHVFG RSLLKSIFTV TRRQLLEKFR
VEKDKLLPEK RTLILTHFPK FLSMLEEEIY GENSPIWEAD FTMPASEGTQ LGHHTVISPA
AVSGSPALPK GLSSMSSLGS MESGGAEPIT GEKRKVPEAL TLEDAKRIRV MGDIPMELVN
EVMMTITDPA AMLGPETNLL TPNAARDETA RLEERRGIIE FHVIGNSLSQ KSNKKILMWL
VGLQNVFSHQ LPRMPKEYIT RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA
VTSNEQVKGY GTHLMNHLKE YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG
YIKDYEGATL MECELNPRIP YTELSHIIKR QKEIIKKLIE RKQSQIRKVY PGLTCFKEGV
RQIPVESIPG IRETGWKPSI KDKGKEVKDP DVLYNMLKNL LAQIKTHPDA WPFMEPVKKS
EAPDYYEIIR FPIDLKTMTE RLKNRYYVTK KLFIADLQRI ITNCREYNLP DSEYCKCANT
LEKFFYFKLK DGGLIEK
//
