ID   HATB_ARATH              Reviewed;         467 AA.
AC   Q9FJT8; Q8LKJ6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            Short=HAT B;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:O14929};
GN   Name=HAG2; Synonyms=HAT1; OrderedLocusNames=At5g56740;
GN   ORFNames=MIK19.19;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-251, AND NOMENCLATURE.
RX   PubMed=12466527; DOI=10.1093/nar/gkf660;
RA   Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA   Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT   "Analysis of histone acetyltransferase and histone deacetylase families of
RT   Arabidopsis thaliana suggests functional diversification of chromatin
RT   modification among multicellular eukaryotes.";
RL   Nucleic Acids Res. 30:5036-5055(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=16648464; DOI=10.1101/gad.1417706;
RA   Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J., Silva M.,
RA   Neves N., Gross M., Viegas W., Pikaard C.S.;
RT   "Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale
RT   gene silencing in nucleolar dominance.";
RL   Genes Dev. 20:1283-1293(2006).
CC   -!- FUNCTION: Acetylates soluble but not nucleosomal H4 (By similarity).
CC       Acetylates 'Lys-12' of histone H4. {ECO:0000250|UniProtKB:O14929,
CC       ECO:0000269|PubMed:16648464}.
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:O14929};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR   EMBL; AB013392; BAB09892.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96802.1; -; Genomic_DNA.
DR   EMBL; AF512724; AAM70417.1; -; mRNA.
DR   RefSeq; NP_200485.1; NM_125057.4.
DR   AlphaFoldDB; Q9FJT8; -.
DR   SMR; Q9FJT8; -.
DR   BioGRID; 21019; 3.
DR   STRING; 3702.Q9FJT8; -.
DR   iPTMnet; Q9FJT8; -.
DR   MetOSite; Q9FJT8; -.
DR   PaxDb; 3702-AT5G56740-1; -.
DR   ProteomicsDB; 230297; -.
DR   EnsemblPlants; AT5G56740.1; AT5G56740.1; AT5G56740.
DR   GeneID; 835775; -.
DR   Gramene; AT5G56740.1; AT5G56740.1; AT5G56740.
DR   KEGG; ath:AT5G56740; -.
DR   Araport; AT5G56740; -.
DR   TAIR; AT5G56740; HAG2.
DR   eggNOG; KOG2696; Eukaryota.
DR   HOGENOM; CLU_046617_0_0_1; -.
DR   InParanoid; Q9FJT8; -.
DR   OMA; WTCDAND; -.
DR   OrthoDB; 180271at2759; -.
DR   PhylomeDB; Q9FJT8; -.
DR   PRO; PR:Q9FJT8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJT8; baseline and differential.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:TAIR.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.90.360.10; Histone acetyl transferase 1 (HAT1), N-terminal domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR019467; Hat1_N.
DR   InterPro; IPR037113; Hat1_N_sf.
DR   InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR   PANTHER; PTHR12046; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR12046:SF0; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF10394; Hat1_N; 1.
DR   PIRSF; PIRSF038084; HAT-B_cat; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   Genevisible; Q9FJT8; AT.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..467
FT                   /note="Histone acetyltransferase type B catalytic subunit"
FT                   /id="PRO_0000232125"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        283
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   BINDING         249..251
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   BINDING         256..262
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   SITE            207
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
SQ   SEQUENCE   467 AA;  52738 MW;  2B8A0465D6451662 CRC64;
     MVQKQQASAG PGTEPKKRRR VGFSPADTGV EANECIKIYL VSSKEEVDSS DISSVKPVDL
     NDFFDGDGKI YGYQGLKINV WINSISLHSY ADITYQSTIN GDKGITDLKS ALQNIFAETI
     VDTKDEFLQT FSTQRDFIRN MVSNGEVMHA GATDGSSKNA EVVPSDPQVI RMEIGSPNAG
     LLYSRLVPLV LLFVDGSNPI DVTDPDWHLY LLIQKKEEKE DPLYRIVGFT AIYKFYRYPD
     RLRMRLSQIL VLPSFQGKGL GSYLMEVVNN VAITENVYDL TVEEPSEKFQ HIRTCIDINR
     LRSFDPIKPD IDSAVQTLTK GKLSKKAQIP RFTPPLNAIE KVRESLKINK KQFLKCWEIL
     IYLALDPIDK YMEDYTSVIT NHVRTDILGK DIETPKKQVV DVPSSFEPEA SFVVFKSVNG
     EEANTNVQVD ENKPDQEQQL KQLVEERIRE IKLVAEKVSK SGQTLKV
//