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Database: UniProt
Entry: A0DTL9_PARTE
LinkDB: A0DTL9_PARTE
Original site: A0DTL9_PARTE 
ID   A0DTL9_PARTE            Unreviewed;       427 AA.
AC   A0DTL9;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=GSPATT00020067001 {ECO:0000313|EMBL:CAK86386.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK86386.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK86386.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK86386.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107}.
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DR   EMBL; CT868574; CAK86386.1; -; Genomic_DNA.
DR   RefSeq; XP_001453783.1; XM_001453746.1.
DR   AlphaFoldDB; A0DTL9; -.
DR   STRING; 5888.A0DTL9; -.
DR   EnsemblProtists; CAK86386; CAK86386; GSPATT00020067001.
DR   GeneID; 5039568; -.
DR   KEGG; ptm:GSPATT00020067001; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_1_1; -.
DR   InParanoid; A0DTL9; -.
DR   OMA; ILCEVDK; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
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:SF215; HISTONE ACETYLTRANSFERASE OF THE MYST FAMILY 2; 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   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          140..417
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          98..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        321
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   427 AA;  50282 MW;  717745016B9B1C3A CRC64;
     MSAKGKNKAK AFATLPNAVP TSSTKIHEGA LDNSNYVLAQ MKNGKWEKAK IIECRLSKDY
     DPKQKKVDSS YEYYVHYEFY NRRMDEWVGR ERLQLTEDPI IEDTQPKKRP RPSDKREVTA
     ENDEHEGMDQ QSLITHEMHT KFKTIEKIEF GQYRCDTWYY SPFPSGYHNI DCLLICEFCL
     SFYIRKSELQ RHQLKCVLCK LGHPPGDEMY RDTERRLSMF EIDGHKNPTY CENLCYIAKL
     FLDHKNLYYD VEPFLFFVLT EYNETGFHIV GYFSKEKESS QGWNLSCILT FPFHQRKGYG
     KFLISMSYQL SLIEGKYGTP ERPLSDLGRE SYLSWWTQSI IDYLKKNKDG EITIAGLTKE
     TGIKDTDAWW TLEQKHLIKY QQSQPLICMD MAYLDLIYSK AGRPGLPVKK DCIHWVPYKR
     PKGQDKN
//
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