ID   EAF6_YARLI              Reviewed;         135 AA.
AC   Q6C626;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Chromatin modification-related protein EAF6;
GN   Name=EAF6; OrderedLocusNames=YALI0E13079g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC       is involved in transcriptional activation of selected genes principally
CC       by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC       also involved in DNA repair (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG79479.1; -; Genomic_DNA.
DR   RefSeq; XP_503886.1; XM_503886.1.
DR   AlphaFoldDB; Q6C626; -.
DR   SMR; Q6C626; -.
DR   STRING; 4952.CAG79479; -.
DR   EnsemblFungi; CAG79479; CAG79479; YALI0_E13079g.
DR   GeneID; 2912017; -.
DR   KEGG; yli:YALI0E13079g; -.
DR   VEuPathDB; FungiDB:YALI0_E13079g; -.
DR   HOGENOM; CLU_093901_2_1_1; -.
DR   InParanoid; Q6C626; -.
DR   OMA; IEVQIYN; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR   InterPro; IPR015418; Eaf6.
DR   PANTHER; PTHR13476; PTHR13476; 1.
DR   Pfam; PF09340; NuA4; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Coiled coil; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..135
FT                   /note="Chromatin modification-related protein EAF6"
FT                   /id="PRO_0000086900"
FT   REGION          92..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..42
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        94..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  15460 MW;  5019D86013D0421F CRC64;
     MSDQKMNQYE KLKKQLKDNI NKKKTHDKNL NSLEEQIFTL EGAYLEETSH GNLVKGFDTY
     IKGAQSKKRY VFNEDDRLFS LSSAVFLKHQ AKTGAGGDLD ETKNERKKTA SQKRRKGDST
     PMSGDEKPSK RSRVD