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Database: UniProt
Entry: A0A421JC84_9ASCO
LinkDB: A0A421JC84_9ASCO
Original site: A0A421JC84_9ASCO 
ID   A0A421JC84_9ASCO        Unreviewed;       411 AA.
AC   A0A421JC84;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=JA9_000826 {ECO:0000313|EMBL:RLV86713.1};
OS   Meyerozyma sp. JA9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV86713.1, ECO:0000313|Proteomes:UP000286412};
RN   [1] {ECO:0000313|EMBL:RLV86713.1, ECO:0000313|Proteomes:UP000286412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA9 {ECO:0000313|EMBL:RLV86713.1,
RC   ECO:0000313|Proteomes:UP000286412};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) 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}.
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:RLV86713.1}.
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DR   EMBL; NSDU01000008; RLV86713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JC84; -.
DR   STRING; 2028340.A0A421JC84; -.
DR   Proteomes; UP000286412; 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:UP000286412};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RLV86713.1}.
SQ   SEQUENCE   411 AA;  46786 MW;  D054C06ED15BD47E CRC64;
     MTLGEGLAPY LPNDTHFKAL HVYTATYETK SFTCVRKRDK VKPQTFKIKH FLALIDSDQQ
     IILGLELYVY LICTNDSTIS HIFVSKADTT GLSKYKVKVA AIVRAMISYV DNIDIKEYTK
     HVERKKTAVE SARNTEESPV VEAVRSIVDK LRSEPSFYRR LVHDQTNEQT PVFVSSNVIH
     RISLFTRSSE QYLFPESSEN KNKHIINGNQ LLKWWIGILD GLAAPRKWQC YVTIPGSDSE
     SIKKYISDVN GSWNLGSIFD KNEDSPAIYT IPLLPDDPKG RFLEHLVVEG RHKTVTTKAF
     WEELGFRQEF RLGNVVGILG CESSLDTKHG SNKLPRPVKR SQYRQVIKAI KRTDFSDNED
     VSLLVEKEIP NLIGDVYEDA IGTQDTKHSK VQKRSAPVVN NITGLVKRKK Q
//
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