MYST1_ORYSJ
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 03-AUG-2022, entry version 120.
DE RecName: Full=Putative MYST-like histone acetyltransferase 1;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9LXD7};
GN OrderedLocusNames=Os07g0626600, LOC_Os07g43360; 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; 4530.OS07T0626600-01; -.
DR PaxDb; Q8LI34; -.
DR PRIDE; 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; MNMVKYW; -.
DR OrthoDB; 629545at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q8LI34; OS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
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
