ID HAT1_DEBHA Reviewed; 409 AA. AC Q6BSQ1; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 24-JAN-2024, entry version 95. DE RecName: Full=Histone acetyltransferase type B catalytic subunit; DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341}; GN Name=HAT1; OrderedLocusNames=DEHA2D07062g; OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Debaryomyces. OX NCBI_TaxID=284592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC RC 2968; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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. 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; CR382136; CAG86913.2; -; Genomic_DNA. DR RefSeq; XP_458769.2; XM_458769.1. DR AlphaFoldDB; Q6BSQ1; -. DR SMR; Q6BSQ1; -. DR STRING; 284592.Q6BSQ1; -. DR GeneID; 2901027; -. DR KEGG; dha:DEHA2D07062g; -. DR VEuPathDB; FungiDB:DEHA2D07062g; -. DR eggNOG; KOG2696; Eukaryota. DR HOGENOM; CLU_036024_2_1_1; -. DR InParanoid; Q6BSQ1; -. DR OMA; WTCDAND; -. DR OrthoDB; 180271at2759; -. DR Proteomes; UP000000599; Chromosome D. 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; IEA:UniProtKB-SubCell. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0042393; F:histone binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:InterPro. 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..409 FT /note="Histone acetyltransferase type B catalytic subunit" FT /id="PRO_0000227723" FT REGION 53..55 FT /note="Interaction with histone H4 N-terminus" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT REGION 206..208 FT /note="Interaction with histone H4 N-terminus" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT ACT_SITE 266 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT BINDING 231..233 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT BINDING 238..244 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q12341" FT SITE 183 FT /note="Interaction with histone H4 N-terminus" FT /evidence="ECO:0000250|UniProtKB:O14929" SQ SEQUENCE 409 AA; 47711 MW; 2A9794B7363E08C2 CRC64; MSDNSPITSI TAASLQPELW TSSSNDALQI YITDSDGTAL NFHPNFTYPI FGDSEQIFGY RDLVIFLCFD HCTFYPFLNV KYSDKLNDDT LEDPREKLLS YLPESTIFKD EVKWVDSINK EKEGFEIPGE LVGNIFTHGD DKFGIYKLDL KNAQGLELHK RLQILVLLFI EAGSYIDHQD ELWDIYVMYK VTDEKTPSII GFCTAYNYWK YGGFEKFDSN QQEVRKKISQ FIVLPMYQGL KLGGRFYNKL YEYWMQDPRV IEVVVEDPSE SFDDLRDRCD LTRLCQNTIK VASVDLPLIN TEWATKLRQE QKLEKRQFSR LLEMILIYQL EHNLTNITKK QVRLFIKKRL YEKNKEILDG LDEPTRLDKL QTAYASLESD YKRILSGLSL HKRALDSTEG SSKKSKPNV //