ID M7C7H9_CHEMY Unreviewed; 778 AA.
AC M7C7H9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ORFNames=UY3_02241 {ECO:0000313|EMBL:EMP40503.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40503.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 EMBL; KB509732; EMP40503.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C7H9; -.
DR STRING; 8469.M7C7H9; -.
DR eggNOG; KOG1472; Eukaryota.
DR Proteomes; UP000031443; 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-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:UP000031443};
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, ECO:0000313|EMBL:EMP40503.1}.
FT DOMAIN 449..597
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 686..756
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 516
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT BINDING 520..522
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 527..533
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 558..561
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
SQ SEQUENCE 778 AA; 89268 MW; 50E5B7447B1A94AA CRC64;
MMTERLTELP FSQSEQGKGL AGPSTGCGLL LGPWHRLAPR PCCGTRGPPE PGLANDACKC
NGWKNPNPPT APRMDLQQPV TNLSELCRSC GHALADHVSH LENVSEEEIN RLLGMVVDVE
NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMSRPVVEGS LGSPPFEKPN IEQGVFNFVQ
YKFSHLPPKE RQTMYELSKM FLLCLNYWKL ETPSQFRQRS QNDDVATYKV NYTRWLCYCH
VPQSCDSLPR YETTHVFGRS LLKSIFTVTR RQLLEKFRVE KDKLVPEKRT LILTHFPKFL
SMLEEEIYGE NSPIWESDFT MPATEGAQLV PRPAAVNTVA VPSTPIFSKK LGSSSSLSSM
SLDASTTEPV PGEKRKLPES LTLEDAKRIR VMGDIPMELV NEVMLTITDP AAMLGPETSL
LSANAARDET ARLEERRGII EFHVIGNALS QKSNKRILMW LVGLQNVFSH QLPRMPKEYI
PRLVFDLKHK TLALIKDGRV IGGICFRMFP TQGFTEIVFC AVTSNEQVKG YGTHLMNHLK
EYHIKHNILY FLTYADEYAI GYFKKQGFSK DIKVPKGRYL GYIKDYEGAT LMECELNPRI
PYTELSHIIK KQKEIIKKLI ERKQAQIRKV YPGLTCFKEG VRQIPVESIP GIRDTGWRPL
GKEKGKELKD PDQLYNTLKN LLAQIKTHPS AWPFMEPVKK SEAPDYYEII RFPIDLRTMT
ERLKNRYYVT KKLFIADLQR IITNCREYNP PDSDYCKCAN TLEKFFYFKL KEAGLIDK
//
