ID   EAF7_YARLI              Reviewed;         354 AA.
AC   Q6CF40;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Chromatin modification-related protein EAF7;
GN   Name=EAF7; OrderedLocusNames=YALI0B10472g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By 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 EAF7 family. {ECO:0000305}.
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DR   EMBL; CR382128; CAG82967.1; -; Genomic_DNA.
DR   RefSeq; XP_500722.1; XM_500722.1.
DR   AlphaFoldDB; Q6CF40; -.
DR   STRING; 4952.CAG82967; -.
DR   EnsemblFungi; CAG82967; CAG82967; YALI0_B10472g.
DR   GeneID; 2907096; -.
DR   KEGG; yli:YALI0B10472g; -.
DR   VEuPathDB; FungiDB:YALI0_B10472g; -.
DR   HOGENOM; CLU_783488_0_0_1; -.
DR   InParanoid; Q6CF40; -.
DR   OMA; MRCILER; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR012423; Eaf7/MRGBP.
DR   PANTHER; PTHR13581; PTHR13581; 1.
DR   Pfam; PF07904; Eaf7; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; DNA damage; DNA repair; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..354
FT                   /note="Chromatin modification-related protein EAF7"
FT                   /id="PRO_0000215881"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..255
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  38903 MW;  CA6EF5D55927C248 CRC64;
     MVKREDTDDT STQAVDGAEV ESNGQGDAGT DSSPWSIESE TVLFNSLCKF KPVGIHKHFR
     MISLSASLNY YFSESPKDAP VFSHQDVWDK LGTLYDLDGL DELEYVADNQ DSDMDEDEDD
     EAAIEGIAKR SQMKEFVLPF RDYGFLQIEQ ATAVASEQSS PAMSREQSVL EDGPTAGDEK
     KGLADDDDES SDLDELDDEE MKLAETKIKV EGEQQEREEN GGEEEHDTME GSAEPEEAEK
     SEEEGEGEES GESESESGSE SQSDSDAQTG RQRRTRAATA AAVRGRGTSK GKTVRDKKSS
     PSTRASSAPR RSTRRKATTE PEDTATEREE TPTPKKSSGG VKKPAPRRST RRKK