ID   EAF7_KLULA              Reviewed;         402 AA.
AC   Q6CX31;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Chromatin modification-related protein EAF7;
GN   Name=EAF7; OrderedLocusNames=KLLA0A11682g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382121; CAH03096.1; -; Genomic_DNA.
DR   RefSeq; XP_451508.1; XM_451508.1.
DR   AlphaFoldDB; Q6CX31; -.
DR   STRING; 28985.XP_451508.1; -.
DR   EnsemblFungi; CAH03096; CAH03096; KLLA0_A11682g.
DR   GeneID; 2896753; -.
DR   KEGG; kla:KLLA0_A11682g; -.
DR   eggNOG; KOG4051; Eukaryota.
DR   HOGENOM; CLU_685231_0_0_1; -.
DR   InParanoid; Q6CX31; -.
DR   OMA; HKHFHMV; -.
DR   Proteomes; UP000000598; Chromosome A.
DR   GO; GO:0043189; C:H4/H2A histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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..402
FT                   /note="Chromatin modification-related protein EAF7"
FT                   /id="PRO_0000215880"
FT   REGION          92..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..402
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  45723 MW;  9B74FC76319F55B3 CRC64;
     MSAVKIESPR GQTWSKVEEI RLFKWMMLFK PAGIHKHFHM VCLLERLNKP DQYPIKLLQS
     DKGSSDKVFS GEDVWEQLSR YYNLEKADEV ENQPYPEFYN DDGPTETTNK KTEGDAQLDN
     DDDSDNDVDN CDELKRNIIP LQNRLQQETE FELSWEDYGE LMLEHARDHE VEDIKQEETA
     SADDKAKLKG AESQDTQVEQ ESEEPREREK DIDEKDTEQN NVQAKQEMAT TPPVSVGESV
     SELANEPVDE PVDAHKKPRT RRSTRLTRSQ KRGIDDESEN KEDQPHGGNT DEKEDVEHDT
     EGRSGSEKES TADAADTTAT KQVTFADESE GAAKESANSP TGKAEENETE SSQQPRPKKQ
     KVAAAEEVPE DLADVDSPAR RTRRKSITKP TTRLSSRLRS RK