ID   HAT1_ASPOR              Reviewed;         511 AA.
AC   Q2UEX1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   08-NOV-2023, entry version 91.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN   Name=hat1; ORFNames=AO090026000444;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007159; BAE59894.1; -; Genomic_DNA.
DR   RefSeq; XP_001821896.1; XM_001821844.1.
DR   AlphaFoldDB; Q2UEX1; -.
DR   SMR; Q2UEX1; -.
DR   STRING; 510516.Q2UEX1; -.
DR   EnsemblFungi; BAE59894; BAE59894; AO090026000444.
DR   GeneID; 5993924; -.
DR   KEGG; aor:AO090026000444; -.
DR   VEuPathDB; FungiDB:AO090026000444; -.
DR   HOGENOM; CLU_036024_2_1_1; -.
DR   OMA; WTCDAND; -.
DR   OrthoDB; 180271at2759; -.
DR   Proteomes; UP000006564; Chromosome 3.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:InterPro.
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   PANTHER; PTHR12046; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR12046:SF0; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 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..511
FT                   /note="Histone acetyltransferase type B catalytic subunit"
FT                   /id="PRO_0000227718"
FT   REGION          44..46
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   REGION          210..212
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   REGION          455..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        284
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   BINDING         249..251
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   BINDING         256..262
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   SITE            182
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
SQ   SEQUENCE   511 AA;  58620 MW;  276138C26F25C1F4 CRC64;
     MASEGDWTCD ANDAVQITLV QPGEQKPKTL SSFHPQFTYP IFGDDETIFG YKGLIIRLRF
     AAHDLRPHIH ISYDEKFKTV GDTSAVDLIK TLSPFIPEEA FSTLPDYENA VQEDKDAKDF
     VPPGKLVHNY VTRGRTYEIW AASLADPQVR RLLDRAQVFV SLFIEAGTPL ETEDPEWTLE
     RWTVYFVYEK VKPPTPTASQ YSIVGYATTY RWWFYQRDSP EKGTVTNDPF PGPEIRPAQL
     PARLRIAQFL ILPPHQGSGH GTHLYTTIHT ACFNDSTIVE LTVEDPNEAF DALRDTADFH
     ILRPEFLKHN VNINPDPYAE LSKKQRPRRV PTSALIPTKL LHDIRSTYKI ASTQFAHVLE
     MFLLGEIPTK NRHAGGANMS RLLVKKYNAT DPNERRYYWW RMLVKQRLFK RSRDILIQLE
     MSDRIEKLEE TVTNVEEGYE ALIKVFTARE EALMAKQEES GESPETAVLE DSVASSSDSS
     TRDQRTKRKF TVEDEDEEEE GESEVSKRPK V
//