HAT1_YARLI
ID HAT1_YARLI Reviewed; 451 AA.
AC Q6CC99;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, 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=YALI0C11231g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 (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}.
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DR EMBL; CR382129; CAG82023.1; -; Genomic_DNA.
DR RefSeq; XP_501713.1; XM_501713.1.
DR AlphaFoldDB; Q6CC99; -.
DR SMR; Q6CC99; -.
DR STRING; 4952.CAG82023; -.
DR EnsemblFungi; CAG82023; CAG82023; YALI0_C11231g.
DR GeneID; 2909147; -.
DR KEGG; yli:YALI0C11231g; -.
DR VEuPathDB; FungiDB:YALI0_C11231g; -.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; Q6CC99; -.
DR OMA; YFINLDE; -.
DR Proteomes; UP000001300; Chromosome C.
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:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
DR Gene3D; 1.10.10.390; -; 1.
DR Gene3D; 3.90.360.10; -; 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; PTHR12046; 1.
DR Pfam; PF10394; Hat1_N; 1.
DR PIRSF; PIRSF038084; HAT-B_cat; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..451
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000227728"
FT REGION 52..54
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT REGION 202..204
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT ACT_SITE 276
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 241..243
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 248..254
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 451 AA; 52089 MW; 6D491A9BF98D7133 CRC64;
MDIATEWTTN ANEALTITLE PSKGKGKGKE VSNGSEKSHV FNPIFTYPIY GDVETILGYK
NFELNLKMDA STMLPLVTVK FSDKLEFDGI SFDDPVERLL EFLPEETATD EAEWEEKRVK
ELGDGFKPVG KEFGTFSVNS EKYTVHRSTL LDPETLKLHL RLQIFVPLFI EAGSYIDNED
DRWEIYIVYN AEKEIVGFST VYCYWFYEPS AKESKAPKDA SLEQLQKQPF SPTLRKRISQ
YVILPPFQGK GLGGQLYTLL FSRFYADPNV YEITVEDPSE AFDDLRDRCD LKWLADQGFP
SEVFRMLQTT SAHGEKAGDN RTGRTKVVAG AFWTKWLEEH RLKYKLAHRQ FARCFEMILL
ACLEVSSPTK KRNIKDARLF IKKRVYVRNR EFLEELGGKI EVMSKLQETY ESMEEDYARI
MKPVLGYVKD GLKKRDRNDA GNEEAKRVKV E
