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Database: UniProt
Entry: A0A0L7QT97_9HYME
LinkDB: A0A0L7QT97_9HYME
Original site: A0A0L7QT97_9HYME 
ID   A0A0L7QT97_9HYME        Unreviewed;       453 AA.
AC   A0A0L7QT97;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=WH47_02963 {ECO:0000313|EMBL:KOC61706.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC61706.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC61706.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC61706.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ414755; KOC61706.1; -; Genomic_DNA.
DR   RefSeq; XP_017793919.1; XM_017938430.1.
DR   AlphaFoldDB; A0A0L7QT97; -.
DR   STRING; 597456.A0A0L7QT97; -.
DR   EnsemblMetazoa; XM_017938430.1; XP_017793919.1; LOC108575601.
DR   GeneID; 108575601; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000053825; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
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:UP000053825};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOC61706.1}.
FT   DOMAIN          166..444
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          78..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        342
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   453 AA;  52510 MW;  68F4911154894A30 CRC64;
     MIEEHDEHET ICDSVNSLVE GCRLPVRMHG TEDWPLAEII SVKEVHGVKC YYVHYVDFNK
     RLDEWVMEDC LDTRKVQYPR RDGTTPGTGA ATPKKQAVSR PPSPSSLSNE PVNGSAVLQA
     ALQKKMSRKR KATFIENDDS QDGPPQTPGP RPTGSLVAHH HDDIVTRMKN VELIELGRHR
     IRPWYFSPYP QEMVNLPCIY ICEFCLKYRK SRKCLERHLA KCNLRHPPGN EIYRKGSISF
     FEIDGRKNKN YAQNLCLLAK LFLDHKTLYY DTDPFLFYVM TDFDSRGFHI VGYFSKEKES
     TEDHNVACIL TLPPYQRRGY GKLLIEFSYE LSKFEGKTGS PEKPLSDLGL LSYRSYWAHT
     ILDILLNIKP LIENEKPQIT ISEICELTSI KKEDVISTLQ NLNLINYYKG QYIVTLNRDI
     IEQHAAAMEK RQIRIDPKCL HWTPKDWSVR AKW
//
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