ID   EPL1_CANGA              Reviewed;         821 AA.
AC   Q6FLZ0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Enhancer of polycomb-like protein 1;
GN   Name=EPL1; OrderedLocusNames=CAGL0K12386g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61717.1; -; Genomic_DNA.
DR   RefSeq; XP_448754.1; XM_448754.1.
DR   AlphaFoldDB; Q6FLZ0; -.
DR   SMR; Q6FLZ0; -.
DR   STRING; 5478.XP_448754.1; -.
DR   PRIDE; Q6FLZ0; -.
DR   EnsemblFungi; CAG61717; CAG61717; CAGL0K12386g.
DR   GeneID; 2889983; -.
DR   KEGG; cgr:CAGL0K12386g; -.
DR   CGD; CAL0134065; CAGL0K12386g.
DR   VEuPathDB; FungiDB:CAGL0K12386g; -.
DR   eggNOG; KOG2261; Eukaryota.
DR   HOGENOM; CLU_010580_0_0_1; -.
DR   InParanoid; Q6FLZ0; -.
DR   OMA; TYIKFSA; -.
DR   Proteomes; UP000002428; Chromosome K.
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..821
FT                   /note="Enhancer of polycomb-like protein 1"
FT                   /id="PRO_0000214158"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  94601 MW;  E62688EF63CA7619 CRC64;
     MSSNGGSNTN ERSVGPDSGS LRSNSNLSSV NGDGSDSGST RFRHRKISVK QRLRIHLPSD
     LKNLDKNEIQ KRELLDVETG VEKNEEKEVH LHRILQKASV LEHLNSKKDY IPTPDASKTW
     SDYDKFYSGK FVETQAYVKF SVTVEDCCGV PYTLDEIDDD FLENSLNKNS DLKLNEDEFE
     SLCSAFETAI KERQPFLQMD PETILTFDEV KPTLLKVDFN NMHLRSQLAQ EVAAIHNPQT
     ANSSSDGNGP FTTVFDSSTT ANVRPIPELI EKYGKEVYEH WSRRKIEAKG AEIFPQLKFE
     RPGEKEEVDP YVCFRRRELR HPRKTRRVDI LNSQKLRILL KELRHAKDMS LLVAQREQIN
     LQLIEDDLKI LNKRKHVISI KRKLDIKGED EDLINHKRKR PTIMTIEKKR QQEEALAAAK
     RAAEQEKAAA AAKAAEAKNK SKAQKKQNEQ AAKVKSSKQK NSSSQDLTKK VTQEESQSEE
     QQPAMSHVYV KLPSSKIPDI VLEDVEKLLQ NKEKSARRFV QERMARRKLE DNDEFINLTD
     DPHNPVFDLT TLNCSEVPFS PFSSIASSKL KINKSFYLRD LNDYLNGIAT DLKVFNKDGE
     KIEDNKTASG NQNVRKTEVY NPFDSGSELH SREYPVKFRR RFGRGNIEYL DVKRKIDNFS
     DTRFCEFIDF KAIENQELEN NGRNLDVYES RADEFSRLLE KWKFDSTNNE YGLRFSDEPA
     RLNQISNDTQ VIRFGTMLGT KSYEQLKEAT IRYRKDYISR IRQQKLNAQK QQQILQQQQF
     LQQQQENGSP NNATMPINPI NKSTLKQDVA SNVLVGTQQK S