ID G0SGV7_CHATD Unreviewed; 610 AA.
AC G0SGV7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Enhancer of polycomb-like protein {ECO:0000256|RuleBase:RU361124};
GN ORFNames=CTHT_0067730 {ECO:0000313|EMBL:EGS17446.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17446.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988047; EGS17446.1; -; Genomic_DNA.
DR RefSeq; XP_006697064.1; XM_006697001.1.
DR AlphaFoldDB; G0SGV7; -.
DR STRING; 759272.G0SGV7; -.
DR GeneID; 18260811; -.
DR KEGG; cthr:CTHT_0067730; -.
DR eggNOG; KOG2261; Eukaryota.
DR HOGENOM; CLU_010580_1_0_1; -.
DR OMA; HIKWNEG; -.
DR OrthoDB; 1343374at2759; -.
DR Proteomes; UP000008066; 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:UP000008066};
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 7..146
FT /note="Enhancer of polycomb-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10513"
FT REGION 302..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..602
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 70671 MW; 04A6DE5218D4BB78 CRC64;
MSTRKVRYKK LSVKTTLAVL REHQIDPSEY EQLSTEAQIA TGVEQAEENE YHLQTVLKTT
GLAADKEIPV PPPQKSELNY DELYFRTYSK PASYIRFSQT VEESVGCMYD MNEDDEAFLK
EYNKKRPPSA QLSEDDFERI MEVYEETAQI KTPFAAIDQT IVPYDDMLQG LQEIENCKTK
IMPHAKEVYE YWKSRRQASG NKPLQPTIKF ETHQETDDMD PYVCFRRREV RQTRKTRARD
VQSADKLKRL RKELEEGRQL VLASHQRELL KYELLKADRD IYETRLQLKQ QKIRLGIKTD
DEDLVNQKER PAPPKRKASE VPAVQRPPPP TQLRITVRSS DGRPPEQDLA LLSDRLAEKE
NELRADIEKK VQSHSEWNRH HVDLTRGPLS PVRGPQPEVS FRPAKTQYLM TPPASTSSEE
EPMKMDLDKP EFPPHVFQFR GVSQPEQMAE HRPAYPAYRR RIGRLNRLWI DRRGLASPPH
DINPEVADRW KYDQSSDDED EPPQYEVDPF DTRALKFRAS IPLPSWLTAR VALGPRPSLL
PPGHPQHQQL AQAQAQAQHH GQHGQQPHPQ QQQQQQQQQK QPPHPQQPPA PMQSPQPPQQ
QRPQPTAAAA
//
