ID   EPL1_NEUCR              Reviewed;         589 AA.
AC   Q7S747;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Enhancer of polycomb-like protein 1;
GN   Name=epl-1; ORFNames=NCU03834;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002240; EAA31357.1; -; Genomic_DNA.
DR   RefSeq; XP_960593.1; XM_955500.2.
DR   AlphaFoldDB; Q7S747; -.
DR   SMR; Q7S747; -.
DR   STRING; 5141.EFNCRP00000003346; -.
DR   PRIDE; Q7S747; -.
DR   EnsemblFungi; EAA31357; EAA31357; NCU03834.
DR   GeneID; 3876740; -.
DR   KEGG; ncr:NCU03834; -.
DR   VEuPathDB; FungiDB:NCU03834; -.
DR   HOGENOM; CLU_010580_1_0_1; -.
DR   InParanoid; Q7S747; -.
DR   OMA; HIKWNEG; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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..589
FT                   /note="Enhancer of polycomb-like protein 1"
FT                   /id="PRO_0000214164"
FT   REGION          298..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..331
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..589
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  67297 MW;  B6DB1DA8A02C63BF CRC64;
     MATRKVRYKK LSVKTQLAVL REDQIEASEY ESLTSENQIA TGVEQAEENE YHLQAVLKGA
     GVAADQEIPV PPPQQSELDY DQFYPQKVAK TSTYIRFSQT VEECISCLYD MTEDDETFLK
     SYNMKLTPSA RLSEDDFERI MDVYEDMAAN ITPFSAIDQT VPSYQEMLRG LEPLDSTKVM
     VHAKQIYEYW KSRREISKNR PLNPTLKFET HAESDELDPY VCFRRREIRQ TRKTRARDVQ
     SADKLKRLRK ELEEGRQLIL AAHNRELLKA DMLKVERAIF DQRAIIKEQK LRLGIRTGDE
     DLVNQKPQKR KAPEAPSAQR PPPPPQIRMP VRPDGRPAES DLVQLSDRLA EKNAELIIEI
     EKKIQNHIDW NKNYVDLTGK PLSPVQGPRQ DLGFRPAKTQ YLMTPPASAS SGSMDEPTPM
     DLDKPKPNPP PPVKFRGVAQ DEQSLAHPPS YRRRIGRLNR LWIDRRGLPS PARDLSEEQS
     DRWKYDQSSD DEDDAPVYML DPFDTKALRY RASIPLQTVT RPPPPVINRQ FIPPGAVPQQ
     LAQSSFAPGQ PQPQSQPQPN QSQSLPLPQP QQPVAQPQPQ PQPQAQPVS