ID A0A074VTZ5_9PEZI Unreviewed; 542 AA.
AC A0A074VTZ5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=M437DRAFT_52748 {ECO:0000313|EMBL:KEQ61167.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ61167.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ61167.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ61167.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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}.
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DR EMBL; KL584839; KEQ61167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VTZ5; -.
DR STRING; 1043003.A0A074VTZ5; -.
DR HOGENOM; CLU_511984_0_0_1; -.
DR OrthoDB; 2787984at2759; -.
DR Proteomes; UP000030672; 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:UP000030672};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 365..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59867 MW; 77508CF935A23BBE CRC64;
MEEDQSAQSR TELYSRLEKV LGAGSRYKIH HLSTRPTKSD ALFAAAPATR PQRTKCESHF
LTLAVASPSS STNSQTQSGH VFAFAIEVLV YTTSSLTTLF VSKADSTGYL SSSPTKSSLS
PIRPLTSTFI TWLAESRQRP GIPLVVSLFA RAQDQYLFPG SVDHGAKHVL DDRQLVKWWC
KTLDPVLRHD TADQAYTTRA HVIVPGFDSY ETTQFFPPSY RSDPPDNRKW RHGHPLLDIA
PYPSAPPRCL VPHFPDDPKA RYLDELDAEI PDSQPSQSWF SPSKKGNGMW KSIRTLDQFW
DTMAFRQECS SGRMVGFIWL VFTPTQPTIQ SLEDSVTNLT PATSFNADDL LGADQIFSSQ
ESLGQAAEVK KSSPRKSARR KKLTGPIIPR QPKIKSTSSN LSSKSFKAAS KEWPERGRGQ
ILLDHASYTR VHDLLLRLDF QDIGAATSST RKWLGEVTAI TTPTSDWGKE VVGAHEIAEK
KSIAEGALPS VPGQVNDLSS MLVRKKRKNA DDGAQAPAPA EAPAVNVLGA NMIRKKPKVN
KP
//
