ID A0A1Y3MW98_PIRSE Unreviewed; 1609 AA.
AC A0A1Y3MW98;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Enhancer of polycomb-like protein {ECO:0000256|RuleBase:RU361124};
GN ORFNames=PIROE2DRAFT_15115 {ECO:0000313|EMBL:OUM59365.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM59365.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM59365.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM59365.1,
RC ECO:0000313|Proteomes:UP000195826};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-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; KZ151111; OUM59365.1; -; Genomic_DNA.
DR STRING; 73868.A0A1Y3MW98; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
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.
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:UP000195826};
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 10..159
FT /note="Enhancer of polycomb-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10513"
FT REGION 344..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1609 AA; 173866 MW; 1FCA8323B5DA03A7 CRC64;
MSYKSGTKFR SRKIDNKRPL AVYRSSELQD LNELTNLSRA APMVATGVEK EEEEEYHLQN
ALHSTQSGVA HHTTFIPTPD ASRLINNYSD FYNKPFHQPK SLIRHSIPME EAIGCLYNMD
EQDDIFFAEY MKELKEGKIK EEAKINEDQF EEVMYALENL TNQKFGDELS TLEELQEYMN
TQLHPPPSAC YHYIFEYWKK RRLQRNKKPI QPYLKTEELK IDSDPYVCFR RREIKTLRKT
RRCDALSLEK LKRLQGEMEQ AHQLMEMVCK REKLRRESLL LEHKIFEQKI LIRQMKKKLG
VVSSDKAQNE TDNSMLPLSE NNSYKANSAN VNSGISINVP GTQANVNNSS SAGHTGHTRV
RKKMRKSHHY TGDEPSAKRL TIPKIKIRQS SVLHTEEGGR SASEKAAQAE INSRNAKKTE
EEKAGWIDLM DLPDPTEDLP FTHQGNVYYQ PDLPLSIDYK TFSLRSSQHL PFARRRIGRG
GRIIFDRRVS LQKIREIKKL HKRSIGLLGQ PGSYEGRFYS HGGKGKTKPK LPWLKNAYPQ
RRESVDYQWF DELSDLDDFD SEEEIREDTT TLAYNAGIYN EADQMVLHVK PAFPEQFNPQ
FSMKRNMIPN NIHHSTPTNQ PSSTNINSNS ASSAQVAGVT NSSMSSISNP LGKTNLSHSS
SISNTQTNTA VLSMSQNQSS PVLQTPHKTP TPATTHIQPS TTPKTSKMAN ANTTPGATTI
TTPSLTTTAT SATILANGHI SPVSKINGIG TPNNPASGLP SSAIDPTAAL LQSSAGSVSN
KTHITTPVMA VGSPAMKVNV NGVAINALNQ QSTITNAKYT PTMNPQTSPS NLSVKTMPNG
LAANTLHANA NNAAIASTLT TANKSPTPSA ATAAAVVAAN NKAMTNLMAN ANAKTMASPK
VIPTMNPMTA AALKNNTINT MNANTINAVN AMNPLNAMNA MNQMNAMNKM KLAQGYGASP
VNDPNINLEG LKNQSYLAQA TKGQRISSPY NAAAKTAALN PYNLAGVNAN ALANAKMNSY
YNTALKGNAA AAAANALALN GKAGVTAQGN ATAAGSFALT ANQLKAVNEA QKAQALQTAT
AKATTPPSTV PAAATTSATV NATTVAMTTK AAVAATVAQT PTLPASLQPT TVSTTTTPLM
KPNTANPLVA VNAANSAELM MASSPRTTPN SVKSTARKTI RKDTPTMNAT TTLKSAQSTP
KSKPTVEDPK ALNIRQLMQA QAQAQAQAQE YAALEQNQLK QRLQQAIGSE AAVASHLHTV
NATSTAQATA AAGIVNQTVI NNPTAAAATA INGTHATPHV NPTNTINISN LSAGAAEINA
AAAAAQTSPM ISTANSHIPQ NLKNVLLNSQ QNNLIHEGNM NVFAGAGLSP QKNLSNLTLV
NNLAAQRQQQ QQNKLLMTAA AANQGVVGLG QANLLQNPNL QQQQQLRMLR LQQLRGVVPN
AAAMNSNISL QQQQALLYRQ QQQQQQILNA LQRQNMVGMP GMPMMVGPNG LPKGVAANGS
PPRQFVQPGF LPQYQQAAQQ QRNLMMMQQI KMMNNKQLAE QGLGNNAALM MGFNGLGGVP
ASAANQILMN QRAGLAANGL VGTKEDIAKA AALMTVIKYQ TELTKYKKQ
//