EAF3_YARLI
ID EAF3_YARLI Reviewed; 387 AA.
AC Q6C9M9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Chromatin modification-related protein EAF3;
GN Name=EAF3; OrderedLocusNames=YALI0D09845g;
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: 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}.
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DR EMBL; CR382130; CAG80821.1; -; Genomic_DNA.
DR RefSeq; XP_502633.1; XM_502633.1.
DR AlphaFoldDB; Q6C9M9; -.
DR SMR; Q6C9M9; -.
DR STRING; 4952.CAG80821; -.
DR EnsemblFungi; CAG80821; CAG80821; YALI0_D09845g.
DR GeneID; 2910924; -.
DR KEGG; yli:YALI0D09845g; -.
DR VEuPathDB; FungiDB:YALI0_D09845g; -.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; Q6C9M9; -.
DR OMA; GLQTYFD; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII 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:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
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; IPR000953; Chromo/chromo_shadow_dom.
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 SMART; SM00298; CHROMO; 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..387
FT /note="Chromatin modification-related protein EAF3"
FT /id="PRO_0000088782"
FT DOMAIN 100..126
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 211..385
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 52..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 43183 MW; 1D6B1FD49435AEA7 CRC64;
MVLATNSRCL AYHGPLLYEA KILMSYDPSK RGSKAKVEDG LPPTVEIGNV VNTHKRKRGP
RASLPAAGAT PDGDDSNDKN RHFSPKEGKP DVPADLADEN EDKICYYVHY KGWKNTWDEW
VGEERVLALN EDNIKLQKEL KAAALAAAKK GKDFDALAPP EALSETASPA PTTKRKSMAS
KDSPAEGPRP VKRRGGLAAL EDLEKEDDYL KRKEIALVVP DKLKAQLVDD WEFVTKDHQL
VGLPRKVTVV DILKEFKKEA EAKYRPGSAD ADILNEVVSG IKLYFDRSLG SILLYRFERE
QYLQITQSPD HSNKTMSEVY GAEHLLRLFV SLPGLIAMTN MDAQSVAVLK EHLEDFVRFL
STHQKTYFLK EAYTNASPAY EALSKGL
