ID   MYST1_ORYSJ             Reviewed;         450 AA.
AC   Q8LI34; Q0D4H1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Putative MYST-like histone acetyltransferase 1;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9LXD7};
GN   OrderedLocusNames=Os07g0626600, LOC_Os07g43360;
GN   ORFNames=OJ1339_F05.128;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Histone acetyltransferase which may be involved in
CC       transcriptional activation. {ECO:0000250|UniProtKB:Q9LXD7}.
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:0000250|UniProtKB:Q9LXD7};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- PTM: Autoacetylation at Lys-274 is required for proper function.
CC       {ECO:0000250|UniProtKB:Q9H7Z6}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR   EMBL; AP004009; BAC07072.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF22252.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT02740.1; -; Genomic_DNA.
DR   RefSeq; XP_015644713.1; XM_015789227.1.
DR   AlphaFoldDB; Q8LI34; -.
DR   SMR; Q8LI34; -.
DR   STRING; 39947.Q8LI34; -.
DR   PaxDb; 39947-Q8LI34; -.
DR   EnsemblPlants; Os07t0626600-01; Os07t0626600-01; Os07g0626600.
DR   GeneID; 4343971; -.
DR   Gramene; Os07t0626600-01; Os07t0626600-01; Os07g0626600.
DR   KEGG; osa:4343971; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_1_1; -.
DR   InParanoid; Q8LI34; -.
DR   OMA; ILCEVDK; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   CDD; cd18642; CBD_MOF_like; 1.
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: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.
DR   Genevisible; Q8LI34; OS.
PE   3: Inferred from homology;
KW   Acetylation; Activator; Acyltransferase; Chromatin regulator;
KW   Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..450
FT                   /note="Putative MYST-like histone acetyltransferase 1"
FT                   /id="PRO_0000238466"
FT   DOMAIN          63..122
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          174..445
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         207..232
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ACT_SITE        350
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         317..319
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         324..330
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         354
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   MOD_RES         274
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
SQ   SEQUENCE   450 AA;  51104 MW;  18BABF1963015A34 CRC64;
     MGSMEASTAP ENGTAAAAAA AASTACNGAG GGGGAAAASN GGGVERRLRS SAASASWASH
     LPLEVGTRVM CRWRDQKLHP VKVIERRKSS TSSSPADYEY YVHYTEFNRR LDEWVKLEQL
     DLETVETDVD EKVEDKATSL KMTRHQKRKI DETHVEQGHE ELDAASLREH EEFTKVKNIA
     KIELGRYEID TWYFSPFPPE YNDSPKLFFC EFCLNFMKRK EQLQRHMKKC DLKHPPGDEI
     YRSGTLSMFE VDGKKNKVYG QNLCYLAKLF LDHKTLYYDV DLFLFYVLCE CDDRGCHMVG
     YFSKEKHSEE SYNLACILTL PPYQRKGYGK FLIAFSYELS KKEGKVGTPE RPLSDLGLLS
     YRGYWTRVLL EILKKHKSNI SIKELSDMTA IKADDILSTL QSLDLIQYRK GQHVICADPK
     VLDRHLKAAG RGGLEVDVSK LIWTPYKEQG
//