ID A0A401T3C9_CHIPU Unreviewed; 880 AA.
AC A0A401T3C9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=chiPu_0015631 {ECO:0000313|EMBL:GCC37130.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC37130.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC37130.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000256|ARBA:ARBA00008607}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC37130.1}.
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DR EMBL; BEZZ01000945; GCC37130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401T3C9; -.
DR STRING; 137246.A0A401T3C9; -.
DR OMA; GIQETGW; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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-EC.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 551..699
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 788..858
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 90..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 618
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT BINDING 622..624
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 629..635
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 660..663
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
SQ SEQUENCE 880 AA; 100069 MW; D2F759837BA47159 CRC64;
MRFNADAAPE TTTPMMPRLG LNENVITFNT DYLRRGVDYS SQVASRVASA RCRLRLVAMA
AGEEKAGVRV KRGVSSRLMA EAAQASQARA QAPYPSPCQA QLQAAASPSP AAPSPADPAR
PGASSSQQRS VQRKAQVRAF PRAKKLEKLG VFSACKANDT CKCNGWKNPN PPTAPRMDIQ
QPAASLCEPC RSCGHTLADH VSHLDNVSED EINRLLGMVV DVENLFMSVH KEEDTDTKQV
YFYLFKLLRK CILQMARPVV EGKLGSPPFE KPSIEQGIFN FVQYKFSHIP AKEKQTMYEL
SKMFLLCLNY WKLETPSQFR QRSQNEDVDA YKVNYTRWLC YCHVPQSCDS LPRYETTQVF
GRTLLRSIFT VTRRQLLEKF RVEKDKLMPE KRTLILTHFP KFLSMLEEEI YGQSSPIWDS
DFTLSAAEGV QLGQQTAVSP SPVPSIPTSS RNINCSSSPA SISVEMGVSE PEPGEKRKMS
DTMTLEDAKR MRVMGDIPME LVNEVMLTIT DPAAMLGPET NLLSANAARD EAARLEERRG
VIEFHVIGNS LSQRSNKKIM MWLVGLQNVF SHQLPRMPKE YITRLVFDPK HKTLALIKDG
RVIGGICFRM FPTQGFTEIV FCAVTSNEQV KGYGTHLMNH LKEYHIKHNI LHFLTYADEY
AIGYFKKQGF SKDIKVPKTR YVGYIKDYEG ATLMECELNP KIPYTELSHI IKKQKEIIKK
LIERKQAQIR KVYPGLTCFK EGVRQIPIES IPGIQETGWK PSGKEKGKEL KDPDQLHNSL
KNLLAQIKSH PSAWPFMEPV KKSEAPDYYE IIRFPIDLKS MSDRLKNRYY VSKKLFIADV
QRIITNCREY NPPESEYCKC ANMLEKFFYF KIKEMGLLDK
//
