ID   EPL1_YARLI              Reviewed;         839 AA.
AC   Q6CEV5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Enhancer of polycomb-like protein 1;
GN   Name=EPL1; OrderedLocusNames=YALI0B12584g;
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. 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; CR382128; CAG83058.1; -; Genomic_DNA.
DR   RefSeq; XP_500807.1; XM_500807.1.
DR   AlphaFoldDB; Q6CEV5; -.
DR   STRING; 4952.CAG83058; -.
DR   PRIDE; Q6CEV5; -.
DR   EnsemblFungi; CAG83058; CAG83058; YALI0_B12584g.
DR   GeneID; 2907028; -.
DR   KEGG; yli:YALI0B12584g; -.
DR   VEuPathDB; FungiDB:YALI0_B12584g; -.
DR   HOGENOM; CLU_010580_0_0_1; -.
DR   InParanoid; Q6CEV5; -.
DR   OMA; TYIKFSA; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..839
FT                   /note="Enhancer of polycomb-like protein 1"
FT                   /id="PRO_0000214166"
FT   REGION          350..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  93202 MW;  523CEC1298020230 CRC64;
     MAKAAKAAGS SARFRQRKIS VKQTLAVLKQ SDIPDLEEEQ QRELQQIETG VEKGEEEEHH
     LQAAINSSIA QSTGAKVEKI YIPTPDASQV WKEYDRFYSS SFHEPASYIR TSVTVEETSG
     CLYNMDDEDA EFLKTCKPPI SEDDFEEVMH RFEVTISEKQ PFVSIDVSNL LSFEEMAQHI
     EDGIRQVQED PTSPEYILAQ LQSSLGITVN GTKGKNEGKA FLATFKKIGA VIYPHWRARK
     VERKGQSIVP HLKFEDHEKD DSDPYVCFRR RELRQVRKTR RTDVLSIERL RRMQAEMETA
     KQLVEMVATR EFTRKAALKA EWDVFEDRCA IKTLKRELGI KGEDEDLVAQ KKRKVEPKKE
     EKAEKASTPV RGGKAAGSAA SAQAAAAQAA AAGSGSPSVS STHVPPNVSI PPSKIPNMDL
     ITIAQVVRDK DEAIAKAVRE KLRLRADADR DWHNLTNSGY IPYCEYLNAE VSSSGEPPVP
     QYSSINEMAY FEKHNASHRY TTKSDFNKDL ASMVGNKPFA DAQVYGAIVG DDGELRLSDA
     TSTSSPVDRV IPRSSFMSMR KRVGRGGRMW MDRRGLQRNT VLKPSSLAKN SLDDTAESEA
     DEVAMERLAD RQKYDRETEP TRQMSSYDKD PSQLNGISSD TQSIRFGSML LSKAYENYRE
     VFQQRQQQLM MLQQQILQQQ QQQQMRNRQQ SHPPGDPGAG LGGGQGAGGG AGGSRNNSPA
     PGTNGPQSKM HNAAPMGYNK QGMTPSQHQQ YQQMQQQQQQ QQQQQQQRKM GVAPMNAASA
     AAAMAAQPRR SSGSPDGQRF NGLPNGGAMA NGVLPNGMSQ RMMPGGDMKQ KSELAKVDA