ID   HAT1_CANGA              Reviewed;         388 AA.
AC   Q6FKS5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN   Name=HAT1; OrderedLocusNames=CAGL0L09042g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
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; CR380958; CAG62139.1; -; Genomic_DNA.
DR   RefSeq; XP_449169.1; XM_449169.1.
DR   AlphaFoldDB; Q6FKS5; -.
DR   SMR; Q6FKS5; -.
DR   STRING; 284593.Q6FKS5; -.
DR   EnsemblFungi; CAGL0L09042g-T; CAGL0L09042g-T-p1; CAGL0L09042g.
DR   GeneID; 2891100; -.
DR   KEGG; cgr:CAGL0L09042g; -.
DR   CGD; CAL0135094; CAGL0L09042g.
DR   VEuPathDB; FungiDB:CAGL0L09042g; -.
DR   eggNOG; KOG2696; Eukaryota.
DR   HOGENOM; CLU_036024_2_1_1; -.
DR   InParanoid; Q6FKS5; -.
DR   OMA; HNANECI; -.
DR   Proteomes; UP000002428; Chromosome L.
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: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:EnsemblFungi.
DR   CDD; cd04301; NAT_SF; 1.
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; 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; 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; 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.
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..388
FT                   /note="Histone acetyltransferase type B catalytic subunit"
FT                   /id="PRO_0000227720"
FT   DOMAIN          142..306
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          197..199
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   ACT_SITE        258
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   BINDING         223..225
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   BINDING         230..236
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   SITE            177
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
SQ   SEQUENCE   388 AA;  45819 MW;  7D26B0E7E97840D4 CRC64;
     MSIDDFKPEK WTISSNEALK LSLVSEDNAI QFSPTFTYPI FGTEEQIFGY KDLVIHLAFD
     AITFKPFLNV KFSSKFEGSE EELVNIKEKL LEYLPIDDTI YKDEEKWIDS FKKEQESIEA
     YKNDQNIDEY KIDNADFEIY KVNLQDPKMK RFHRRIQIFS LLFIEAASYI DEDDPKWEIF
     IVQTKKDKKF VGYATAYNYW YYPGANNFDS ESKYRYRGKI SQFLILPPYQ GRGHGSHLYN
     SIVKNWRNDS SILEIVVEDP NESFDDLRDV NDLEMLYKDG FFNKLPQERP IPNAWIESTR
     LKYKIEKRQF SRLLEMILLS TGSNNFEYQV KQRLLIKNKD GLEGMEVSDI KDALNKSFES
     LREDYDRILG KCQFSNDADG PSKKKIKT
//