ID A0A178DST4_9PLEO Unreviewed; 580 AA.
AC A0A178DST4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=IQ07DRAFT_590382 {ECO:0000313|EMBL:OAL46867.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL46867.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL46867.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL46867.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441653; OAL46867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DST4; -.
DR STRING; 765867.A0A178DST4; -.
DR InParanoid; A0A178DST4; -.
DR OrthoDB; 2787984at2759; -.
DR Proteomes; UP000077535; 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:UP000077535};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 349..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 64735 MW; F66732AE9B20EF52 CRC64;
MTNEHTSKPL KDLLAEQLPK DVPFTFHHYS TPPTKSSALF SAPPHGKSER TYCESHFLAA
SITQKETAAS ALPVELLILA IEVLIYTTRN LTTIFVSKAD STGYLSELQL PRSQAGSPLK
VICGTFVSWL ARERQREGKK LVISLFARAQ DQYLFPASIE NKKKHVLDDR GLVRWWCKVL
DPIIWQYKAE DERKPFAERL LQAESAAVGT WSQTDATAKG YLVIPGFDPY ETLRYIPQPS
QPNTTRRWAS THPLLQIAPH PAAPPRCLVP HFPDDPKSRF LDELDEELPD RGTDAMVVEG
GTPSRSNGQW KSVKTLDQFW EFMAFRQECS SGRIVGFIWV VITPPQPSIP EEDEVSLSQQ
SLSQTLSDEM PKKANPSPKK QKRNKRRQEP RIKYGPIPLV LPKIKTSSSN LSATSNASST
SSAKALPEKS PYYSWPINSR GTVCFSARNY NRAHEVLLQQ SFANRRATAQ STKKWKEEIG
VLGGMEDWSW TVIGKKEEST ASVTSTNRVM PTVVMGVRKK RKPDAESSAT QINGTTVVQT
LGEGLVRKKA KIEPLQASEP NADGVNMLSA NLVRKKGTVP
//
