ID G9P4J2_HYPAI Unreviewed; 578 AA.
AC G9P4J2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=TRIATDRAFT_251300 {ECO:0000313|EMBL:EHK41980.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK41980.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK41980.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:0000256|ARBA:ARBA00024456};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000256|ARBA:ARBA00024456};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK41980.1}.
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DR EMBL; ABDG02000027; EHK41980.1; -; Genomic_DNA.
DR RefSeq; XP_013940221.1; XM_014084746.1.
DR AlphaFoldDB; G9P4J2; -.
DR STRING; 452589.G9P4J2; -.
DR GeneID; 25778672; -.
DR eggNOG; KOG4534; Eukaryota.
DR HOGENOM; CLU_511984_0_0_1; -.
DR OMA; DQLWVGQ; -.
DR OrthoDB; 2787984at2759; -.
DR Proteomes; UP000005426; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010484; F:histone H3 acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR016849; Rtt109.
DR PANTHER; PTHR31571; ALTERED INHERITANCE OF MITOCHONDRIA PROTEIN 6; 1.
DR PANTHER; PTHR31571:SF2; HISTONE ACETYLTRANSFERASE RTT109; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR SMART; SM01250; KAT11; 1.
DR PROSITE; PS51728; RTT109_HAT; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 351..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 64104 MW; 6FCAEB8F9E54FF62 CRC64;
MASADPPDAG LRGRLAAVLP KGYKFGIHHV STPPTKVDAL YSAPPGERPE RTYCEKHFLS
VSIDAENSSS DASTSENTPE QAAQRKRVLI LGIEIFIYTT ARSTTLFVSK ADSTGFLNKL
QLPKGAPSPI REVCATFVRY LVDKRRRKDV QLVVSLFARA QDQYLFPGSI EYSGKHVLDD
RGLVKWWCRV LDPIVESPPR GSLSAWRNTK GYLLIPGLDA YETRAFIPRR AGATSSWALS
HPLERISHYS REFDWVPPRC LIPKFPDDPK CRFRDELDDE VTKTKAMKTT GSWKSVKTLD
MFWEMMAFRQ ECSSGRMTGF IWVVFDDLDD ESKQDGSDIV SVSSASVVTS ALSGAPETPR
KQRTLSNVTP ATTPRRLFPS KSDQNKKSKK RKAAKIKRKL RGPIKSRQPR IKTKQRNYLL
DKPVSTAYYY WPHHGRGERI VDETDYKRMH ELLLRLDFAT LDKATGSTRR WLSEVGLGSR
WGFDVTGTRE LAAASAETTE GGAAPVNNLS GLVKRKRSDT VGDGSQGEAA SAGVNVLGGG
LVRKKPKQGE GEGDGGVADT TPPVNVLSAG LVRKKQKT
//
