ID   EPL1_KLULA              Reviewed;         806 AA.
AC   Q6CIN8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Enhancer of polycomb-like protein 1;
GN   Name=EPL1; OrderedLocusNames=KLLA0F25146g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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. Involved in gene silencing by neighboring
CC       heterochromatin, blockage of the silencing spreading along the
CC       chromosome, and required for cell cycle progression through G2/M (By
CC       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 enhancer of polycomb family. {ECO:0000305}.
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DR   EMBL; CR382126; CAG98909.1; -; Genomic_DNA.
DR   RefSeq; XP_456201.1; XM_456201.1.
DR   AlphaFoldDB; Q6CIN8; -.
DR   SMR; Q6CIN8; -.
DR   STRING; 28985.XP_456201.1; -.
DR   PRIDE; Q6CIN8; -.
DR   EnsemblFungi; CAG98909; CAG98909; KLLA0_F25146g.
DR   GeneID; 2895178; -.
DR   KEGG; kla:KLLA0_F25146g; -.
DR   eggNOG; KOG2261; Eukaryota.
DR   HOGENOM; CLU_010580_0_0_1; -.
DR   InParanoid; Q6CIN8; -.
DR   OMA; TYIKFSA; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0000786; C:nucleosome; IEA:EnsemblFungi.
DR   GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   InterPro; IPR024943; Enhancer_polycomb.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   PANTHER; PTHR14898; PTHR14898; 1.
DR   Pfam; PF10513; EPL1; 1.
PE   3: Inferred from homology;
KW   Cell cycle; DNA damage; DNA repair; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..806
FT                   /note="Enhancer of polycomb-like protein 1"
FT                   /id="PRO_0000214163"
FT   REGION          403..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  93398 MW;  366DD96D89139DFD CRC64;
     MPAPAVDSSR FRHRKISVKQ RLRIYKSHEI KDLEQEDVSA ISSQHQQREL MEIETGVEKN
     EEKEEHLYKI LQSNQLRENK KDLFIPTPDA SKTWDEFDRF YQGEFKCPTS YIQFSAQLED
     CCGTLYNMDE EDEIFLADLN KSLADSVEPL TEDEFELIMA NFESSIKDRQ PFLSMDPESI
     LSFADLKPTM LKNDVGDSGV KKELAKEIGM PEDEPFLTMF DNKRPLGKRE KNMETLIELF
     GEKIHDHWKQ RKISRHGCDI FPQLKSERNN DKDDNDPYVC FRRRELRQPR KTRRIDVQNS
     QKLRLLCQQL EYTKDLALTV AKRERAVLEV LENEKFVFQA RAQLKTMKRK LGIDADNEDL
     YSAKKQKLVS SVRTIKQQQQ LLLQKQLQIQ QQQQQQLQQQ QAAITSDSSV KRAKSSKSSK
     LHKEDSGLYA DEKGSEPKKK GPKTGSNKNK EQSLSSAQEI GAQSPVANVS NVQQQQKQAS
     SQVYVKLPNS KIPDIVLEDV GKLLHSKEKS TRKFVEDRMR KRKQEDGDIF FNLTDDPYNP
     VFNLSIPDNV SPQDAPFSSV AGSKFEVKTS YYSPNLQNYI TGTANDIKVF NKEGEAVENN
     EYKKLEFFNP FDNEIHTHSR EFPIAFRRRR GRFNMEYIDQ RKTDHNINDM LLQFIDLDGI
     QKQELDNDVI NVYDSKLDDL SRSYYHWKYD SNYNIYGSKF SDEPAKLNQI SNDTQVVRFG
     TMLGSKAYEQ LRDATIKYRQ EQINKRKKLN SLQQQQMLQK GQQPINNAPH SQSSSPPSHQ
     DTRKNPGSTP NQSSPPKKHV TPNAAA