ID G8C128_TETPH Unreviewed; 427 AA.
AC G8C128;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=TPHA0N00750 {ECO:0000313|EMBL:CCE65856.1};
GN OrderedLocusNames=TPHA_0N00750 {ECO:0000313|EMBL:CCE65856.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65856.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65856.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE612869; CCE65856.1; -; Genomic_DNA.
DR RefSeq; XP_003688290.1; XM_003688242.1.
DR AlphaFoldDB; G8C128; -.
DR STRING; 1071381.G8C128; -.
DR GeneID; 11532053; -.
DR KEGG; tpf:TPHA_0N00750; -.
DR eggNOG; KOG4534; Eukaryota.
DR HOGENOM; CLU_050421_0_0_1; -.
DR OMA; FLEHLIV; -.
DR OrthoDB; 2787984at2759; -.
DR Proteomes; UP000005666; Chromosome 14.
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 PIRSF; PIRSF027124; Histone_acetylase_Rtt109; 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:UP000005666};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 427 AA; 49302 MW; 19E541CB0BBA3479 CRC64;
MRLEKILSDC LPSDDRFEVL HLQSVPTENY PIVTKKLGQD NELITVKTQH FFTLFQNSKT
VFGLEIYVYI TLIKKAKLDT NNDVLDAERL IFISKADTTG YNNKRINIKL ITKSIIHYLL
SIDPNYYLQK VKPLKRNYVG KFSNYISKST STVKALKLLS KRKSAHQKQL YPPNDLFLHL
KCEQNIVTKI CLFTRPADQY LFADSSKNAK KHVLTGEGLL LWWISIMDDL LIEEYESGTE
AKLNIPGEEN VRIRKYFRNL KYSSWNIGDI FGGSANSLAV FNIPLFPDDP KSRFLHQLVE
ENRIYKTDME TFWIELQERQ EFKAGITVSV IGISGHLRSI SKNIPMDGEI IKTPSKSSFK
HLKSYITGEE FDTEEGALES YSNIKEYVVS RMHKDLLTVS GTYQFKPKIK PSVQKFTITT
LQPRRAK
//
