HAT1_MAGO7
ID HAT1_MAGO7 Reviewed; 468 AA.
AC G4N7S6;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000269|PubMed:30776962};
GN Name=HAT1 {ECO:0000303|PubMed:30776962}; ORFNames=MGG_06375;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATG3; ATG9; GSK1 AND SSB1,
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-8, AND
RP MUTAGENESIS OF SER-8.
RX PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT pathogenicity in Magnaporthe oryzae.";
RL Autophagy 15:1234-1257(2019).
CC -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
CC complex. Has intrinsic substrate specificity that modifies lysine in
CC recognition sequence GXGKXG (By similarity). Involved in DNA double-
CC strand break repair (PubMed:30776962). Required for appressorium turgor
CC pressure, autophagy and conidial nuclear degradation (PubMed:30776962).
CC During the germination process and upon starvation conditions,
CC translocates from the nucleus to the cytoplasm where it acetylates ATG3
CC at 'lys-262' and 'Lys-267', thus influencing autophagy through
CC controlling ATG3-ATG8 interaction (PubMed:30776962). Also acetylates
CC ATG9 at 'Lys-621' to regulate ATG9 binding to vesicles, which is also
CC important for autophagy and pathogenicity (PubMed:30776962).
CC {ECO:0000250|UniProtKB:Q12341, ECO:0000269|PubMed:30776962}.
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:0000269|PubMed:30776962};
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). In
CC the nucleus, interacts with GSK1 and SSB1 (PubMed:30776962). In the
CC cytoplasm, interacts with ATG3 and ATG9 (PubMed:30776962).
CC {ECO:0000250|UniProtKB:Q12341, ECO:0000269|PubMed:30776962}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30776962}. Cytoplasm
CC {ECO:0000269|PubMed:30776962}. Preautophagosomal structure
CC {ECO:0000269|PubMed:30776962}. Note=Is only present in the nucleus
CC under nutrient-rich condition, and translocates from the nucleus to the
CC cytoplasm with the assistance of SSB1 during germination or upon
CC starvation. {ECO:0000269|PubMed:30776962}.
CC -!- PTM: Phosphorylated at Ser-8 by GSK1 in the nucleus which impairs its
CC translocation to the cytoplasm through interfering the interaction
CC between HAT1 and SSB1. Dephosphorylation under nutrient starvation
CC conditions promotes the interaction between HAT1 and SSB1 and results
CC in the translocation of HAT1 from the nucleus to the cytoplasm in order
CC to acetylate ATG3 and ATG9. {ECO:0000269|PubMed:30776962}.
CC -!- DISRUPTION PHENOTYPE: Significantly attenuates virulence toward rice
CC leaves by affecting appressorial penetration and infectious hyphal
CC growth (PubMed:30776962). Impairs the acetylation of ATG3 during
CC germination and weakens the interaction between ATG3 and ATG8
CC (PubMed:30776962). Abolishes also the acetylation of ATG9 and thus
CC impairs the ATG9 binding ability to vesicles during nutrient starvation
CC induction (PubMed:30776962). {ECO:0000269|PubMed:30776962}.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; CM001234; EHA50880.1; -; Genomic_DNA.
DR RefSeq; XP_003717199.1; XM_003717151.1.
DR AlphaFoldDB; G4N7S6; -.
DR SMR; G4N7S6; -.
DR STRING; 318829.MGG_06375T0; -.
DR iPTMnet; G4N7S6; -.
DR EnsemblFungi; MGG_06375T0; MGG_06375T0; MGG_06375.
DR GeneID; 2684530; -.
DR KEGG; mgr:MGG_06375; -.
DR VEuPathDB; FungiDB:MGG_06375; -.
DR eggNOG; KOG2696; Eukaryota.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; G4N7S6; -.
DR OMA; YFINLDE; -.
DR OrthoDB; 708105at2759; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Acyltransferase; Autophagy; Chromatin regulator; Cytoplasm; DNA damage;
KW DNA repair; Germination; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response; Transferase; Virulence.
FT CHAIN 1..468
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000447267"
FT REGION 44..46
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT REGION 208..210
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT REGION 442..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 248..250
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 255..261
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT SITE 180
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30776962"
FT MUTAGEN 8
FT /note="S->A: Impairs phosphorylation of HAT1, and promotes
FT the interaction with SSB1 and translocation from the
FT nucleus to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:30776962"
FT MUTAGEN 8
FT /note="S->D: Mimics constitutive phosphorylation and
FT impairs phosphorylation of HAT1, interaction with SSB1 and
FT translocation from the nucleus to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:30776962"
SQ SEQUENCE 468 AA; 53988 MW; D3CF26876BE8F7CF CRC64;
MAESDLWSVD ANSALELSLV EPTEDGLTTV TRFHPRFTYP LFGEEEQIFG YQDLKINLQY
HAPDMRPNVK ITHSKKFKSI GETQPTDLDA LLQGYLPPVA FAKKREFEDA IRLMPADWTP
PGEILSEFDG VDGAKFEIRR SNLADDASRQ IIDRVQLLIL LFIEGGSYIG TDTTDSLDRW
DIFFLYNIKP STTDGTSRYQ FAGYSTVYKF FPLQRFPLEP KEAHENLELP SGEFPFSNLR
SRTRISQFLI LPPFQKSGNG SRLYRTIYDY CLRDPNVIEV TVEDPNEAFD DMRDVADLDF
LRQKSEFTDL RINTDIHIPK QGAAPRGVVD EVKSEEARCL YRIAPRQFSR VLEMHLMSRL
AETVRPTLVD DKVVAKPTKI ETHEYDLWKL FVKQRLYRHN KEVLSQLDRH DRIERLNETL
GSVELEYARI LALAERRTQA TSSNLKRKLD DDENTEGSSS KKARVEDA
