HAT1_KLULA
ID HAT1_KLULA Reviewed; 390 AA.
AC Q6CN95;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN Name=HAT1; OrderedLocusNames=KLLA0E14344g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR EMBL; CR382125; CAG99681.1; -; Genomic_DNA.
DR RefSeq; XP_454594.1; XM_454594.1.
DR AlphaFoldDB; Q6CN95; -.
DR SMR; Q6CN95; -.
DR STRING; 28985.XP_454594.1; -.
DR PRIDE; Q6CN95; -.
DR EnsemblFungi; CAG99681; CAG99681; KLLA0_E14301g.
DR GeneID; 2893933; -.
DR KEGG; kla:KLLA0_E14301g; -.
DR eggNOG; KOG2696; Eukaryota.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; Q6CN95; -.
DR OMA; YFINLDE; -.
DR Proteomes; UP000000598; Chromosome E.
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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR Gene3D; 1.10.10.390; -; 1.
DR Gene3D; 3.90.360.10; -; 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 InterPro; IPR013523; Hist_AcTrfase_HAT1_C.
DR PANTHER; PTHR12046; PTHR12046; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF10394; Hat1_N; 1.
DR PIRSF; PIRSF038084; HAT-B_cat; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000227725"
FT DOMAIN 138..290
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 42..44
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT REGION 193..195
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT ACT_SITE 256
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 221..223
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 228..234
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 390 AA; 45913 MW; 72EED909A3E6390D CRC64;
MAVDLRPETW TVSSNEALNL SLVDENGAVN FKPTFTYPIY GDSEQIFGYK NLQIFLAFDS
ITFKPFVNVK YDAKLNNEIE DVQKLLLDKL PEDDVIIKDE EAWIKTFTKE QETFALPEKD
KLVEEYEIGD QEFVIYRVSL QDPAIKMLHK RMQIFTLLFI ESASYIDEND SSWEIFIVFN
KNSKKCIGYT TTYQFWKYLG AQSFDSSKAD EQKCRAKISQ FLIMPPYQGH GHGKRLYQAI
VKQWMNDLSV VEITVEDPNE SFDDLRDRCD FERVINKNSL ADCPNELPIN IDWITKKQAQ
LKLEKRQFMR ILEMFLLYQK SPNYRLQLKK RIYEKNFEAL MDMDESLKKD KLQTAFQSLT
EDYNRILSKV AIRKRTFSDS QGESDKRLKA
