ID HAT1_EREGS Reviewed; 391 AA. AC Q750F5; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2013, sequence version 2. DT 24-JAN-2024, entry version 112. DE RecName: Full=Histone acetyltransferase type B catalytic subunit; DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341}; GN Name=HAT1; OrderedLocusNames=AGL001W; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 312. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B) CC complex. Acetylates 'Lys-12' of histone H4 which is required for CC telomeric silencing. Has intrinsic substrate specificity that modifies CC lysine in recognition sequence GXGKXG. Involved in DNA double-strand CC break repair. {ECO:0000250|UniProtKB:Q12341}. 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:Q12341}; CC -!- SUBUNIT: Component of the HAT-B complex composed of at least HAT1 and CC HAT2. The HAT-B complex binds to histone H4 tail (By similarity). CC {ECO:0000250|UniProtKB:Q12341}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016820; AAS54489.2; -; Genomic_DNA. DR RefSeq; NP_986665.2; NM_211727.2. DR AlphaFoldDB; Q750F5; -. DR SMR; Q750F5; -. DR STRING; 284811.Q750F5; -. DR EnsemblFungi; AAS54489; AAS54489; AGOS_AGL001W. DR GeneID; 4622964; -. DR KEGG; ago:AGOS_AGL001W; -. DR eggNOG; KOG2696; Eukaryota. DR HOGENOM; CLU_036024_2_1_1; -. DR InParanoid; Q750F5; -. DR OMA; WTCDAND; -. DR OrthoDB; 180271at2759; -. DR Proteomes; UP000000591; Chromosome VII. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi. DR GO; GO:0042393; F:histone binding; IEA:InterPro. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi. DR Gene3D; 1.10.10.390; -; 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; IPR019467; Hat1_N. DR InterPro; IPR037113; Hat1_N_sf. DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su. DR InterPro; IPR013523; Hist_AcTrfase_HAT1_C. DR PANTHER; PTHR12046; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1. DR PANTHER; PTHR12046:SF0; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1. DR Pfam; PF21184; HAT1_C_fung; 1. DR Pfam; PF10394; Hat1_N; 1. DR PIRSF; PIRSF038084; HAT-B_cat; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. PE 3: Inferred from homology; KW Acyltransferase; Chromatin regulator; Cytoplasm; DNA damage; DNA repair; KW Nucleus; Reference proteome; Transferase. FT CHAIN 1..391 FT /note="Histone acetyltransferase type B catalytic subunit" FT /id="PRO_0000227716" FT REGION 193..195 FT /note="Interaction with histone H4 N-terminus" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT REGION 372..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 254 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT BINDING 219..221 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT BINDING 226..232 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT SITE 173 FT /note="Interaction with histone H4 N-terminus" FT /evidence="ECO:0000250|UniProtKB:O14929" SQ SEQUENCE 391 AA; 45208 MW; FC2A69642885E61D CRC64; MAEELKPELW TTSSNSALKL SLVNDENAVQ FSPIFTYPIF GQAEQLFGYQ DLNILLAFDS VTFKPFLNIK YTKKLERGLD DVEGSILKFL PEGDVILKDE VEWVDAFNGE REKFALPNSE SKVAEYTSGG ESFAIFKVHL SDPNIRQLHR RMQIFTLLFI EAASYIDEDD SAWDIFMTFN TSTRQCIGYT TTYKHWRYIN GQEFDSSEKT TKRAKISQFI IFPPYQSKSH GSHLYSAAID VWSKEEKISE VTVEDPNEAF DDLRDRCDFM RLSGSGLSSS IPEDVPIPRT WLTEQARKYK LSLVQFTRLV EMILLYDNSP NFEIQVKARL YQKNHEVLTG MDSDTRKAKL QEAFTSLKED YARILQKVPN RRRVLPSDEE NAGESKRHKK E //