ID B3S7S8_TRIAD Unreviewed; 408 AA.
AC B3S7S8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
GN ORFNames=TRIADDRAFT_50853 {ECO:0000313|EMBL:EDV21249.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV21249.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV21249.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV21249.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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|RuleBase:RU361211};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
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DR EMBL; DS985254; EDV21249.1; -; Genomic_DNA.
DR RefSeq; XP_002116216.1; XM_002116180.1.
DR AlphaFoldDB; B3S7S8; -.
DR STRING; 10228.B3S7S8; -.
DR EnsemblMetazoa; TriadT50853; TriadP50853; TriadG50853.
DR GeneID; 6757524; -.
DR KEGG; tad:TRIADDRAFT_50853; -.
DR CTD; 6757524; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011815_2_2_1; -.
DR InParanoid; B3S7S8; -.
DR OMA; RIRNVEC; -.
DR OrthoDB; 118560at2759; -.
DR PhylomeDB; B3S7S8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0072487; C:MSL complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 121..399
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 58..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 408 AA; 47473 MW; 4613F3E853A80336 CRC64;
MPVRMSTENE WPMAEVVSRR DLGNGEFEYY VHFIDYNKRL DEWVHEKRLN FARMTYPKDG
KKSTSSLPAS PNNKKVNGIG RKRKAVEIAP TIENGQEIKE GPPPKSGSLR QTNADGSDVI
TRMKNIDVIE FGRYQIKPWY FSPYPEQLTR ANVIFICEFC LKYIGSPSAF ARHRDKCKLY
HPPGNEIYRK GKLSFFEVDG RKNKIYCQNL CLLAKLFLDH KTLYYDTEPF LFYILTEFDN
KGFHTVGYFS KEKESSEDYN VACILTLPPY QRKGYGKVLI EFSYVLSKFE GKLGSPEKPL
SDLGLLSYRS YWSQAILEIL SKYLDESNGS TPNITINEIC DATSMRKEDV ISTLQHLDLI
RYYKGQYILT LSKDIIDGHC RSFSKRKVRI DSKCLIWTPK DWAKRGRW
//
