ID A0A2V5IHR4_9EURO Unreviewed; 818 AA.
AC A0A2V5IHR4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=BP00DRAFT_438764 {ECO:0000313|EMBL:PYI28030.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI28030.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI28030.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI28030.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ825557; PYI28030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IHR4; -.
DR Proteomes; UP000248817; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..818
FT /note="histone acetyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016092575"
FT REGION 613..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 89551 MW; DE78F9538F4D39D9 CRC64;
MVLSRSLLAA ASAFLLGSPT EAAGAVTELQ SVLKNTHMSN EYGYPTDFTR GVMPIPVHSH
NDYWRDIPFY SGLSKGCIST EADVWLYNGT LYVGHDESSL TEKRTLESLY INPILDVLQR
QNPTSRFVTS PTRNGVFDTD TSQTLYFFID LKTSGPETLD AVIKALEPLR ARGYLTTLKD
NATITEGPVT VIGTGNTPLD LVGPVANRDY FFDAPLDRLD EDQFADVTGL ISPIASTNFV
AAVGPLSHRK DGQLFGGLSW NFGGGFQFYL SVYASCEIFP VSDLLAEVLP AGVKLTIRHV
SSTPTPCPAL FAAPPGETSE PTFCENHFLT ASVDAEGKDG AEIIVLGVEV LIYSTAHLTT
IFVSKADSTG FLHLLQSAPK VSLLRRISQA FLSFLVRTHQ RPGVRLVVSL FARAQNQYLF
PGSIENEGKH VLDDRGLIKW WCRVFDPILR EYEPESGSHE KNALDRQTES AQSSATAFLI
VPGCDKFETR GFFPSAARLD SQERPRWRNS YPLHQLCDDP KAPPRCLVPR FPDDPKTRFL
IDLDDELPPQ SGEDGKSSVA PGQWRSVRSL DQFWEMMSFR QECSSGRLVG FLWLVINPPG
LVNSVQMTSS RSVLGDLPEP QSNDALASSL EQPEASEGPS VAQPTDPSGP QPTAETLSVS
ESTAQRTADA SAFFWPEAGR GHAVLSEADY KAAIDFLIEQ DFFNQEVSIA STRAWGEKIA
SLADQLWVGQ QVLGRGRTDN PSQQTTEVNT LISSTLVRKR KKVEDEPAQT QVIEKTADEP
APDANAPTAD ATVSTPLPES TSGVNVLQAN LIRKKKKT
//
