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Database: UniProt
Entry: A0A3Q4HYP9_NEOBR
LinkDB: A0A3Q4HYP9_NEOBR
Original site: A0A3Q4HYP9_NEOBR 
ID   A0A3Q4HYP9_NEOBR        Unreviewed;       499 AA.
AC   A0A3Q4HYP9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JAN-2026, entry version 35.
DE   RecName: Full=Histone acetyltransferase KAT5 {ECO:0000256|ARBA:ARBA00073520};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE   AltName: Full=60 kDa Tat-interactive protein {ECO:0000256|ARBA:ARBA00075576};
DE   AltName: Full=Histone acetyltransferase HTATIP {ECO:0000256|ARBA:ARBA00078544};
DE   AltName: Full=Lysine acetyltransferase 5 {ECO:0000256|ARBA:ARBA00081819};
DE   AltName: Full=Protein 2-hydroxyisobutyryltransferase KAT5 {ECO:0000256|ARBA:ARBA00076578};
DE   AltName: Full=Protein acetyltransferase KAT5 {ECO:0000256|ARBA:ARBA00076154};
DE   AltName: Full=Protein crotonyltransferase KAT5 {ECO:0000256|ARBA:ARBA00078969};
DE   AltName: Full=Protein lactyltransferase KAT5 {ECO:0000256|ARBA:ARBA00077013};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000027386.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000027386.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSNBRP00000027386.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-
CC         lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:137954; Evidence={ECO:0000256|ARBA:ARBA00047752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC         Evidence={ECO:0000256|ARBA:ARBA00047752};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-
CC         lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:61996, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:19466, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:231527,
CC         ChEBI:CHEBI:231528; Evidence={ECO:0000256|ARBA:ARBA00047411};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997;
CC         Evidence={ECO:0000256|ARBA:ARBA00047411};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-
CC         hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+);
CC         Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:131780, ChEBI:CHEBI:144968;
CC         Evidence={ECO:0000256|ARBA:ARBA00047557};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC         Evidence={ECO:0000256|ARBA:ARBA00047557};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone]
CC         + CoA + H(+); Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00048940};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000256|ARBA:ARBA00048940};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107}.
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DR   AlphaFoldDB; A0A3Q4HYP9; -.
DR   Ensembl; ENSNBRT00000028103.1; ENSNBRP00000027386.1; ENSNBRG00000020811.1.
DR   GeneTree; ENSGT00940000162343; -.
DR   Proteomes; UP000261580; Unassembled WGS sequence.
DR   Bgee; ENSNBRG00000020811; Expressed in mesonephros and 9 other cell types or tissues.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:TreeGrafter.
DR   GO; GO:0031981; C:nuclear lumen; IEA:UniProtKB-ARBA.
DR   GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IEA:TreeGrafter.
DR   GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR   GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR   GO; GO:0120300; F:peptide lactyltransferase (CoA-dependent) activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901701; P:cellular response to oxygen-containing compound; IEA:UniProtKB-ARBA.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:TreeGrafter.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.10.10:FF:000022; Histone acetyltransferase; 1.
DR   FunFam; 2.30.30.140:FF:000013; Histone acetyltransferase; 1.
DR   FunFam; 3.30.60.60:FF:000001; Histone acetyltransferase; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.630.30; -; 2.
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; IPR050603; MYST_HAT.
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:SF219; 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   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          254..490
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          70..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        389
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   499 AA;  57335 MW;  7FBFCCB326AF494B CRC64;
     LTQPAVEIVE GCRLPVLRKN QEHEDEWPLA EILSVKEVSG RKLYYVHYID FNKRLDEWVT
     TERLDMKKLQ FPKKDAKTPT KNGLSGSRPS SPERERDRER EREKSLDLNV QTATAPSRGK
     TLPTPKRKVE PAPVAPQVPP VIPVPSLPSS AEATQAAVFP AVRETPTFKS REDHELTTNG
     NARRLIPAPP GRKRKANCGG TDEMIKVLQY NKPQSASVFL PPPEDSQDSS DGIPTAPRMT
     GSLVSDRSHD DIVTRMKNIE CIELGRHRLK PWYFSPYPQE LTSLPILYLC EFCLKYLKSL
     KCLQRHLTKC NLRHPPGNEI YRKGTISFFE IDGRKNKNYS QNLCLLAKCF LDHKTLYYDT
     DPFLFYVMTE YDSKGYELSK VEGKTGTPEK PLSDLGLLSY RSYWSQTILE ILMDLKPDNG
     ERPQITINEI SEITSVKKED VISTLQYLNL INYYKGQYIL TLSEDIVEGH ERAMQKRHLR
     IDPKCLHFTP KDWSKRGKW
//
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