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EPL1_ASPFU
ID   EPL1_ASPFU              Reviewed;         582 AA.
AC   Q4WDF1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Enhancer of polycomb-like protein 1;
GN   Name=epl1; ORFNames=AFUA_6G04530;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000012; EAL85587.1; -; Genomic_DNA.
DR   RefSeq; XP_747625.1; XM_742532.1.
DR   AlphaFoldDB; Q4WDF1; -.
DR   SMR; Q4WDF1; -.
DR   STRING; 746128.CADAFUBP00009114; -.
DR   PRIDE; Q4WDF1; -.
DR   EnsemblFungi; EAL85587; EAL85587; AFUA_6G04530.
DR   GeneID; 3505203; -.
DR   KEGG; afm:AFUA_6G04530; -.
DR   eggNOG; KOG2261; Eukaryota.
DR   HOGENOM; CLU_010580_1_0_1; -.
DR   InParanoid; Q4WDF1; -.
DR   OMA; HIKWNEG; -.
DR   OrthoDB; 806707at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
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: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; Coiled coil; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..582
FT                   /note="Enhancer of polycomb-like protein 1"
FT                   /id="PRO_0000214156"
FT   REGION          323..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          238..295
FT                   /evidence="ECO:0000255"
FT   COILED          352..385
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        545..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  66417 MW;  2629F25A7AB902D5 CRC64;
     MGRTRPKKLT SKASIPIVRE HEIDIIDDEV QNALQQVETG VEKAEESEFH LQAAISATAQ
     GKVNEAHIPT PETVLSNLRY DELYPPIFSQ PATYIRFSST IEDCCGCPYN MTEEDDVFFK
     IMNEKREPSN RITEDQFEEV MYFFEETAQT KQPFAAVDSP PVLSFAEMQD SMDATVEESV
     KCFAKDIYEH WKLRRIATGN RPLLPSLKFE TGQDTDDTDP YVCFRRREVR QIRKTRGRDA
     QSADKLRRLR KELEDARQLV ALVRQRELAR KEMLSMERQI FLQRSEVKEM KRKLNIKDDD
     EDLINQKVTS IPARLPHAFA NLPEQPKKKP AEAPAAQRPT APQIRMPQKP GTQAADDMQL
     LEDVQAEKEN EILRDIKQNI AKHIKWNEGY VDYTRAPLSP PPEKTFQAAF RPAITTQLPT
     PPSSDSSDNM MLESALDTAN SLSFRDKLVP RTWEMNEDTC RIPSFRRRIG RGGRLMIDRR
     NMASRCRIEM DPLKADRFKY DREDSDDESE FECDPYDVQI MQHRAIMAAK ARDQAAAAAQ
     AHAQAQAQKR LQAEQTTTNN GPPNIGHTMG SNPGPGAVAS TS
 
 
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