HAT1_ASPOR
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 03-AUG-2022, entry version 87.
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; YFINLDE; -.
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 assembly; IEA:InterPro.
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 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..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
