ID   HAT1_GIBZE              Reviewed;         477 AA.
AC   Q4I6A4; A0A0E0SDI1; I1RSW8; V6RNJ9;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN   Name=HAT1; ORFNames=FGRRES_07254, FGSG_07254;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
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; DS231666; ESU13485.1; -; Genomic_DNA.
DR   EMBL; HG970335; CEF84494.1; -; Genomic_DNA.
DR   RefSeq; XP_011326992.1; XM_011328690.1.
DR   AlphaFoldDB; Q4I6A4; -.
DR   SMR; Q4I6A4; -.
DR   STRING; 229533.Q4I6A4; -.
DR   GeneID; 23554341; -.
DR   KEGG; fgr:FGSG_07254; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G24355; -.
DR   eggNOG; KOG2696; Eukaryota.
DR   HOGENOM; CLU_036024_2_1_1; -.
DR   InParanoid; Q4I6A4; -.
DR   OrthoDB; 180271at2759; -.
DR   Proteomes; UP000070720; Chromosome 4.
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: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:InterPro.
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; 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; 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..477
FT                   /note="Histone acetyltransferase type B catalytic subunit"
FT                   /id="PRO_0000227724"
FT   REGION          44..46
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   REGION          215..217
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   REGION          444..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        290
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   BINDING         255..257
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   BINDING         262..268
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   SITE            189
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
SQ   SEQUENCE   477 AA;  54380 MW;  B353317F4741E1D8 CRC64;
     MEDTTQWLSD ASTAIHISLV SPSESGLQHV ATFNPRHTYS IFGDDEKIFG YQDLKVNLRY
     RANDMRPHLN ISYSKKSGTI NELEPTDVAA ILDEGNHLPK IAFAKARDFE ESSKQLSDDW
     TPPGKLHTTF DSPEGQYEIW CGNLADPAVK QLNSRLQIFV PLFIEGGTYI GQDPDEDSAE
     LDLSDADRWT FFSLYQKRKV GDKTAYVFVG YSTIYRFYYF QPPTPPASPQ SDEWELPNGN
     MDLGELPCRT RLSQFIILPP FQGKGNGARL YKTIFEHYHK IPQTYEFTVE DPNEAFDDLR
     DICDLQFLRK MPEFNNLLVD TNIKIPKKGF LPKLIIGSSL LEEIRLRAKI APRQFGRVLE
     MHLMSKLPVS VRPTMAIEDQ PAATKADQHE AKVWGLIVKQ RLYRHNKEVL SQIEPAERVE
     KLDDTLHGVG LEYARILAAV DRSDKYEGQT TASSKRKLDA DEITEDLSNK KARVEDA
//