RT109_ASPFL
ID RT109_ASPFL Reviewed; 564 AA.
AC A0A364LXP7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Histone acetyltransferase rtt109 {ECO:0000303|PubMed:33823938};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q07794};
GN Name=rtt109 {ECO:0000303|PubMed:33823938};
GN ORFNames=CA14_002973 {ECO:0000312|EMBL:RMZ42713.1},
GN G4B11_009108 {ECO:0000312|EMBL:QMW45653.1};
OS Aspergillus flavus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5059 {ECO:0000312|Proteomes:UP000275480};
RN [1] {ECO:0000312|Proteomes:UP000275480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA14 {ECO:0000312|Proteomes:UP000275480};
RA Chang P.-K., Mack B.M., Scharfenstein L., Gilbert M.K.;
RT "Identification of spontaneous genetic mutation associated with occurrence
RT of a yellow conidial color mutant of Aspergillus flavus.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:QMW45653.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF13 {ECO:0000312|EMBL:QMW45653.1};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=CA14 {ECO:0000305};
RX PubMed=33823938; DOI=10.1186/s43008-021-00060-4;
RA Sun R., Wen M., Wu L., Lan H., Yuan J., Wang S.;
RT "The Fungi-specific histone Acetyltransferase Rtt109 mediates
RT morphogenesis, Aflatoxin synthesis and pathogenicity in Aspergillus flavus
RT by acetylating H3K9.";
RL IMA Fungus 12:9-9(2021).
CC -!- FUNCTION: Histone chaperone-dependent acetylase that modifies 'Lys-56'
CC of histone H3 (H3K56ac) (PubMed:33823938). Histone H3 'Lys-56'
CC acetylation may be required for S-phase-linked DNA damage tolerance (By
CC similarity). Also acetylates 'Lys-9' of histone H3 (H3K9ac)
CC (PubMed:33823938). Autoacetylates (By similarity).
CC {ECO:0000250|UniProtKB:Q07794, ECO:0000269|PubMed:33823938}.
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:Q07794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q07794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, 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:Q07794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000250|UniProtKB:Q07794};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07794}. Vacuole
CC {ECO:0000269|PubMed:33823938}.
CC -!- DISRUPTION PHENOTYPE: Severely decreases acetylation of 'Lys-56' and
CC 'Lys-9' of histone H3 (PubMed:33823938). Increases mycelial branching
CC (PubMed:33823938). Severely decreases spore formation and abolishes
CC sclerotia production (PubMed:33823938). Decreases aflatoxin production
CC (PubMed:33823938). Increases sensitivity to sodium chloride (osmotic
CC stress), hydrogen peroxide (oxidative stress), methyl methane sulfonate
CC (genotoxic stress), and Congo Red (cell wall stress) (PubMed:33823938).
CC Decreases cell population growth rate (PubMed:33823938). Decreases
CC virulence on maize seed (PubMed:33823938).
CC {ECO:0000269|PubMed:33823938}.
CC -!- SIMILARITY: Belongs to the RTT109 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01064}.
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DR EMBL; QQZZ01000104; RMZ42713.1; -; Genomic_DNA.
DR EMBL; CP059863; QMW45653.1; -; Genomic_DNA.
DR SMR; A0A364LXP7; -.
DR VEuPathDB; FungiDB:AFLA_098450; -.
DR VEuPathDB; FungiDB:F9C07_11583; -.
DR Proteomes; UP000275480; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:InterPro.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR016849; Rtt109.
DR PANTHER; PTHR31571:SF2; PTHR31571:SF2; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR SMART; SM01250; KAT11; 1.
DR PROSITE; PS51728; RTT109_HAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; Nucleus; Transcription; Transcription regulation;
KW Transferase; Vacuole.
FT CHAIN 1..564
FT /note="Histone acetyltransferase rtt109"
FT /id="PRO_0000453549"
FT REGION 355..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 138
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 157..159
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 167
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT MOD_RES 263
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
SQ SEQUENCE 564 AA; 61534 MW; CB19F88B6FA59F4E CRC64;
MSKVDVDLGD LLAKVLPTGV KVTIRHISSA PTPCTALFTP PPGEESESTF CENHFLTVSV
NADEHDGPEI IVFGIEVLVY STAHLTTVFV SKADSTGFLH LLKNAPKVSL IRRISNGFLS
FLVQTHQRPG VRLVVSLFAR AQNQYLFPGS IENSGKHVLD DRGLIKWWCR VVDPILREYE
PESGSHEKGL LDRAMESAKS SATAFLIVPG CDKFETRGFF PGTAKSDDKE RPRWLNSYPL
HQLCDNTDAP PRCLVPRFPD DPKTRFLLDL DDELPQKLEA AGSKEGAGQW RSVKSLDQFW
EMMSFRQECS AGRLVGFLWL VINPPGLVNS VQMTSSRPVF KEKAEGSLTT TVPVYDKVDS
KPTGTAVSVS TDSQSSDTAK DSTAEATSGG PVQDPSTQTG SLSSETHPKV QPNTDQNAFY
WPEAGRGHAV MSEEDYKTAI NFLLEQDFYN EKVSIASTKA WSEKVASIVD QLWVGQQVTG
RNTSGESADK HAPTTNIINT GLVRKRKKDE PSQATTATSA QKEGCEGNGT VSTAVTAEAS
TTGTNESPGV NVLQANLIRK KKKA
