ID F8Q2M3_SERL3 Unreviewed; 1032 AA.
AC F8Q2M3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Enhancer of polycomb-like protein {ECO:0000256|RuleBase:RU361124};
GN ORFNames=SERLA73DRAFT_161474 {ECO:0000313|EMBL:EGN97434.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(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; GL945482; EGN97434.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q2M3; -.
DR STRING; 936435.F8Q2M3; -.
DR eggNOG; KOG2261; Eukaryota.
DR HOGENOM; CLU_011403_0_0_1; -.
DR InParanoid; F8Q2M3; -.
DR OMA; IYYMDER; -.
DR OrthoDB; 1343374at2759; -.
DR Proteomes; UP000008063; 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:UP000008063};
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 15..217
FT /note="Enhancer of polycomb-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10513"
FT REGION 159..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 114171 MW; FC3718051A3A14FD CRC64;
MPRNHNLGTS TLRNRNRVTN KTRLKVYHGN IDADPLVLDE DEEKARIVST AGVDAEDANE
HHLQAVLSAA SQRHQSVVRS TRGAAEKVST APAAFIPTPD STGVVDNYEE FYPSGRWKDP
VSYIKSSETV DEACAHALVD GFAYFMDERD KEWFDRNNEE ARGEGTSAQG AFSVPGTTTR
SGSTQRSAKA KGKEPDVAQP MVMSEDEFEL IMGLFEKVTH EKTEFLHHGL EQGMTFPPFS
EYQDTFTSPF TPAIFTSFTV PSWIPSSAQL LRLARMIYPY WRERRIERGG HRIIPALNFD
EADVINESYI CFRRREIKAV RKTRASQATS SDKLLRLQSE LSISLELAKS VLTRENIKKD
AAQQAIQVWE KRMEFVNMKR KFSSLGSKED EDLLHDKERV PKKPKVENMN RATGLKLRPR
DSNDLNSPAM QLEALIRPKE RYTMITGAVD RDMARQKERD HQWEDLLTNP YQPSPVPYTQ
RHWKPFFASR STSPSLLGRD EEDDDDTSSH VRYLRIRFAR ARRLCLDRHD SLVKLPALHQ
SSSSGVSDRK AEFMRRMRQF DDDGDEERVS KLHERWRFDD DDSPVVGPEG PDEQDRVLID
DYEPRYLRHA MTLIQDRDQQ DLLNDPTIVL STAEGRHQAV APFRMGMQPP MRREMQAIAR
PYPSGSGIQT SRPLGSLPLS SPLPNGVPIS MQAHVKAMQP PSSVSHLRIS SNGGMRPPMS
SPTAANMAAN NLPSHSSPPH PPTGVATNGV NGVNHNSHIP ADGDSIKLTA AANGAPPNGV
SQAQNEVNMA ANVDVAQPTQ SPVRPKSDNQ HPAAITIPNG YHVTPMNGYP PMANGSPYMH
HANRQHNGLS AQQMQSLKVA FAGQDPNALH ASGRTLPGSY VGHVVPNAQH FNVQLGNNLN
LKLPPTRQWA QLASPSQQQM ALSNDPVAGG MPSPNVHQMA LPARTPSANG SRASGRGTSI
SSMPSSVGHM MGGGQLTSHS VSPHLQHSPP SLSTALTQLP QQSSPHLQTP TLKMASPALQ
HQQPVGNSQG GY
//
