ID   A0A1G4IPX8_9SACH        Unreviewed;       784 AA.
AC   A0A1G4IPX8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Enhancer of polycomb-like protein {ECO:0000256|RuleBase:RU361124};
GN   ORFNames=LADA_0A06172G {ECO:0000313|EMBL:SCU78548.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU78548.1, ECO:0000313|Proteomes:UP000190274};
RN   [1] {ECO:0000313|EMBL:SCU78548.1, ECO:0000313|Proteomes:UP000190274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU78548.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00025513}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU361124}.
CC   -!- SIMILARITY: Belongs to the enhancer of polycomb family.
CC       {ECO:0000256|ARBA:ARBA00008035, ECO:0000256|RuleBase:RU361124}.
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DR   EMBL; LT598460; SCU78548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4IPX8; -.
DR   STRING; 1266660.A0A1G4IPX8; -.
DR   OrthoDB; 1343374at2759; -.
DR   Proteomes; UP000190274; Chromosome A.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; ENHANCER OF POLYCOMB; 1.
DR   PANTHER; PTHR14898:SF0; ENHANCER OF POLYCOMB-LIKE PROTEIN; 1.
DR   Pfam; PF10513; EPL1; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU361124};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU361124}.
FT   DOMAIN          31..178
FT                   /note="Enhancer of polycomb-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10513"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  90347 MW;  EB25800DA992A748 CRC64;
     MARDSLTNGS ANLNGANPPP SASEAANTRF RHRKISVKQR LQVYKVSDLR KLDKDELQQR
     ELMEIETGVD KNEEKEEHLH QILQKNELAR RDLYIPTPDA SRTWQEYPKL YQGSFVEPRT
     YIRFSATVED CCGSSYNMDE RDEEFLQNTF RSNTKGGKGA VTALSENEFE LMCSSFEAAI
     QERQPFLSID PENILSLAEL KPTIFKRDVG DSGIKDRLAQ EIGLRPQQAF ITQFDTAGSQ
     DTRSLATLIG KYGDQVYTHW KNRKIEAHGN SISPQLKFER HGGERDENDP YVCFRRREVR
     QARKTRRVDY QNSHKLRLLD QQLQYTKRLA LLIAKREKLS LDMINDDLRV FEMRRDIKPV
     KRSLGIKGED DSLLVDSRKR KLVSNVVLNA PSETTSKKAR PKLKKSQTEP GQSKSSTSKV
     GKQHQSQAQQ AQHQLAQQQQ QQQQQQQQQQ QLQQLAQQQK QQTNAVAAHV YVKLPSSKIP
     DILLEDADKI LLNQEKTARN YVEERMRKRK LEDGDQFFNL TDDPYNPVFD LSIPANVSAT
     NAPFSSIASS KYDAQKSYYV PRLEDYLDGI SDDVSVFGKD GDRLSNPKHR RIELYNPFMD
     NREVYTRELP FKFRRRVGRL GLEYIDLHKS QGNFTPLSRL INITEVEQQE CENEILDVYD
     SRLDELTRLQ DRWKHTSDYT NYGAKFSHEP ARLNQISNET QTIRFGTMLG TKSYEQLRDA
     TFKYRQEVYH QRRVPKSSIS QKNSKSKDSS PSSNGMSSVP ARTSSSASLK KNAKTKPSHI
     TTVN
//