EPL1_CANAL
ID EPL1_CANAL Reviewed; 753 AA.
AC Q5AAG1; A0A1D8PRL5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Enhancer of polycomb-like protein 1;
GN Name=EPL1; OrderedLocusNames=CAALFM_CR00100CA; ORFNames=CaO19.7529;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW30781.1; -; Genomic_DNA.
DR RefSeq; XP_718685.1; XM_713592.1.
DR AlphaFoldDB; Q5AAG1; -.
DR SMR; Q5AAG1; -.
DR BioGRID; 1222826; 1.
DR STRING; 237561.Q5AAG1; -.
DR PRIDE; Q5AAG1; -.
DR GeneID; 3639732; -.
DR KEGG; cal:CAALFM_CR00100CA; -.
DR CGD; CAL0000195210; EPL1.
DR VEuPathDB; FungiDB:CR_00100C_A; -.
DR eggNOG; KOG2261; Eukaryota.
DR HOGENOM; CLU_010580_0_0_1; -.
DR InParanoid; Q5AAG1; -.
DR OMA; TYIKFSA; -.
DR OrthoDB; 806707at2759; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:CGD.
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:0043967; P:histone H4 acetylation; IC:CGD.
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..753
FT /note="Enhancer of polycomb-like protein 1"
FT /id="PRO_0000214157"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 87442 MW; A424382130726A7F CRC64;
MAAAPPPPAK NQGKAKQHVT GARFRQRKIS VKQPLTIYKQ RDLPTLDSNE LEPSQVHHLN
SNASSSSTQQ PRDLHAVETG VDKNEEEEVH LQQVINAAQK ALLGSKKEEK SSDMYIPTPD
ASRIWPEAHK YYKDQKFKQP ETYIKFSATV EDTVGVEYNM DEVDEKFYRE TLCKYYPKKK
NKSDENNRKC TELEFETICD KLEKTIEARQ PFLSMDPSNI LSYEELSSYI VDQFKSAVKT
SNPYIVTNGG NLEYISTTAL KERLSKEIKY EPFVTIFDKN QMSTSAVRPI PKLFELFGRP
VYDHWKERKI ERKGKTIQPT LKFEDPNSNE KENDNDPYIC FRRREFRQAR KTRRADTIGA
ERIRSMQKSL HRARDLIMSV SEREILKLDN FQAEHELFKA RCATKACKRE LNIKGDEYLF
FPHKKKKIVR TEDEEREKKR EKKKQDQELA LKQQQALQQQ QQQPPQPPQQ APSKQDGTST
SQPYVKLPPA KVPDMDLVTV SLVLKEKNET IKRAVLEKLR KRKEHDKGFI NLTDDPYQPF
FDISTNRAEE LSHIPYSSIA ATHYHQFNTS NYMNDQLKKL LEEKKPLPGV KTFLGSNGEL
VPSKAFPHLS SLLEEKYKAT SGYIERLLQS VETQDFSSYT NGFKDVEPKE TNEPVMAFPQ
RIRRRVGRAG RVFLDHQQEY PQPNFQQDTD RVGGIPDVYC KEDAIKRLQS KWKFDTEYKT
TEPFSLDPSK LNGISPSTQS IRFGSMLLNR TRK