ID   EPL1_CRYNB              Reviewed;         846 AA.
AC   P0CN59; Q55HM9; Q5K767;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Enhancer of polycomb-like protein 1;
GN   Name=EPL1; OrderedLocusNames=CNBN0910;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000066; EAL17264.1; -; Genomic_DNA.
DR   RefSeq; XP_771911.1; XM_766818.1.
DR   AlphaFoldDB; P0CN59; -.
DR   PRIDE; P0CN59; -.
DR   EnsemblFungi; EAL17264; EAL17264; CNBN0910.
DR   GeneID; 4939700; -.
DR   KEGG; cnb:CNBN0910; -.
DR   VEuPathDB; FungiDB:CNBN0910; -.
DR   HOGENOM; CLU_336162_0_0_1; -.
DR   Proteomes; UP000001435; Chromosome 14.
DR   GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IEA:InterPro.
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; IEA:InterPro.
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; Coiled coil; DNA damage; DNA repair; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..846
FT                   /note="Enhancer of polycomb-like protein 1"
FT                   /id="PRO_0000410084"
FT   REGION          169..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          434..490
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        177..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   846 AA;  95346 MW;  63EAA888FB00D8EC CRC64;
     MVAPGRMVTS SRRIGRVTNK TKLIIYRGSD KVDTSAAETV LWDQEAGGAG KDSNKHQHIG
     ATGVESGELL EHHLQAALSS ASLLHSSNKP SSPKSVKEAP AAALNYHIPT PDATGLVSDT
     VFSQLYQRTK YVEPYNFIRF SDTVEESSCG WGGLGYCMDD ADERWLNDFN SKAEGSSGDV
     KSDKEQGRGM RVKGKDREKE KGDAPAPLVI SEDMFEYIMG VFEKYTEENA PMLHTDLSLL
     PPFSAVENMF STPISPAFLP SNEIPKELGD LKACARMARN VYPHWKSRRE QRQGKSILPQ
     LNYDETNDND PYVCFRRRDI RATRKTRRTD NFSIEQFQKL QFELRSAHAL ADRVLTRERE
     KKSLYEAEKE LWEARWKFFE TKRRWPSLGM TSDEEHKITG RPTIVPPIQI PSLSGQTPLT
     SGQSSSHMRK RTDKDREERA QRERYDAQRN AERSGILSGR SNAPDALKER LQALQQKTEE
     MLARKKEQDA HWDDSIDSPY QPLPPSNSVH AFRSLFVLDP CRAQCKDSET GNEILHPESF
     RIRRGRGGIV RLDRRTSIYS HRRGIQPTSP SEYPTWLFPD IAPRRSEKKR PRSIDEVEEE
     MQEQSPKAMR KDLNETWRYD VDRGGAVGVG MGLEEDYDRV IIDDLEAKYI RHRISLLQES
     DCAKLRPDNY ILDQTREALD AAADAKPPPA PIFQKPPAPQ PNPQLLAAHL QQQQMLAQQQ
     QMEQFQRFQL MAQQQAMAQA QAQAQAQAQA QAQAQAQAQV QAQGQGHPQA HLQTHPQGVS
     QPNGVNSPMP NGQQMLPPSD GVKQLKLPPH AVARLGAAMA NANANANGGL HVLQQQQQQH
     AQTSQQ