EPL1_DEBHA
ID EPL1_DEBHA Reviewed; 1016 AA.
AC Q6BNX0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Enhancer of polycomb-like protein 1;
GN Name=EPL1; OrderedLocusNames=DEHA2E18392g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382137; CAG88364.2; -; Genomic_DNA.
DR RefSeq; XP_460100.2; XM_460100.1.
DR AlphaFoldDB; Q6BNX0; -.
DR STRING; 4959.XP_460100.2; -.
DR PRIDE; Q6BNX0; -.
DR EnsemblFungi; CAG88364; CAG88364; DEHA2E18392g.
DR GeneID; 2902479; -.
DR KEGG; dha:DEHA2E18392g; -.
DR VEuPathDB; FungiDB:DEHA2E18392g; -.
DR eggNOG; KOG2261; Eukaryota.
DR HOGENOM; CLU_010580_0_0_1; -.
DR InParanoid; Q6BNX0; -.
DR OMA; TYIKFSA; -.
DR OrthoDB; 806707at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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; DNA damage; DNA repair; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1016
FT /note="Enhancer of polycomb-like protein 1"
FT /id="PRO_0000214160"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 115389 MW; 1744A9E72DCD5C77 CRC64;
MAIHPSKGTG GSKQSNSGAR FRQRKISVKQ PLTIYKQSDL PTLNASNDLE PSQIHHLNSN
ANQQQRDIHA IETGVDKNEE DEVHLQQVIN AAQKVLLGSQ NEDGDKKKDD SDKKTDASVY
IPTPDASRIW TDASKYYNDK SFREPETYIK FSATVEDTVG VEFNMDEIDE EFLKNKLWKN
YPKVKSPKVK SEKLDDTNKE NDNARKCSEV EFEIICDKLE KIIEEKQPFL SMDPSNILSF
KELSAYIIEE FNNSNKDKPY VQLGSNLKYI STTALKEKLS KELSFEPFVT LFDKSLLDQT
STNIVRPIPK LLELFGEPVY EHWKYRKIER KGKQIHPALK FEDPSANEKD NDNDPYICFR
RREFRQARKT RRADTLGAER IRLLQKSMHR ARDLVMSVCR RELIKLENWE TDHAIFKLRS
DAKNLKRVVG VKGDDFLFYP HKRKKIIKVK EEDEDKESSK IKRDKRSRFD SSREGSATSM
PGSATIGTNA INKDRLANGQ VHHTQEASSS SQPYVKLPPS KIPDMGLVTV SLVLKEKNET
IKRAVLEKLR KRKEQDKDFI NVTDDPYQPF FNIATNTKFK NNELKHIPYS SIAATSFHEI
NTTNYISEKL KNLLEEGKKP LPGTKTFRGS NGELIPSKPF PHLSALIQDR IDNSQFNSVS
YIAQLLSNIE NNNFSAYNNG YGQQQQHQHQ ETNRDKTKLS DPIFRLRKRV GRFNRNFVDR
RGLMKRPNDV IDDFLKFDDE GVNDDCDQMD VDSESISKNN VPNVYDSRVD EIKRLDSRWQ
FDNDLTEYDK GLQSPFSLDP SRLNCISDDT QSIRFGSMLL SKSYDLLRDS VHQRQQALVQ
QARMRTLQQQ QRNNKQQAAG QSSGSSSASL GSNTNSNSSI SGQADQGQTN LTNSGITRQG
GANVNGSQTS TTNNTRSSVS GGSMNPKLPT QSSQRSNTNS PLLASQPQGY SQQQKFNKIP
PTSQSQSQSP THAAGQLQTS KMYNKHGSNI TPSNLKGPKF TPANNNQIGG SLPNRK
