EAF3_DEBHA
ID EAF3_DEBHA Reviewed; 316 AA.
AC Q6BT38;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Chromatin modification-related protein EAF3;
GN Name=EAF3; OrderedLocusNames=DEHA2D03784g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: Involved in deacetylation of histones, chromatin assembly and
CC chromosome segregation. May act as a transcriptional oscillator,
CC directing histone deacetylases to specific chromosomal domains.
CC Component of the NuA4 histone acetyltransferase complex which is
CC involved in transcriptional activation of selected genes principally by
CC acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also
CC 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:0000255|PROSITE-ProRule:PRU00972}.
CC -!- SIMILARITY: Belongs to the MRG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382136; CAG86770.1; -; Genomic_DNA.
DR RefSeq; XP_458632.1; XM_458632.1.
DR AlphaFoldDB; Q6BT38; -.
DR SMR; Q6BT38; -.
DR STRING; 4959.XP_458632.1; -.
DR EnsemblFungi; CAG86770; CAG86770; DEHA2D03784g.
DR GeneID; 2901436; -.
DR KEGG; dha:DEHA2D03784g; -.
DR VEuPathDB; FungiDB:DEHA2D03784g; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; Q6BT38; -.
DR OMA; GLQTYFD; -.
DR OrthoDB; 1624495at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
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 Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; DNA damage; DNA repair; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..316
FT /note="Chromatin modification-related protein EAF3"
FT /id="PRO_0000088777"
FT DOMAIN 13..84
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 145..316
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 114..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 36163 MW; AF7F763321D7B8C2 CRC64;
MSGDDAAVFK PNARVLAYHG PLIYEAKVIK IHEKNKTFIE DGEGKHQPIE GGNLPEEYYS
VNAYFVHYKG WKAKWDEWVG PDRILEYNEA NVQAQKELKE QLTKAKIKPK VKAEPAVAST
GTKKRGMPVS SASTVTKKKK TDPNRVNEVS IFMKPELKYI LVDDWEFITK ERKIINIPSS
RPVTVILNDY LQSKKDQDTS HQTMDVINEI MQGLELYFNK SLSLILLYKF ERLQYMNLLK
EHGDDLRPSE LYGVEHLLRL FVALPGLIAQ TTMDSVSINV LVKQSKDILE FITDNMSVYL
NDYVNVSPAY DSLARS