EAF3_CANGA
ID EAF3_CANGA Reviewed; 355 AA.
AC Q6FN68;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chromatin modification-related protein EAF3;
GN Name=EAF3; OrderedLocusNames=CAGL0K02321g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61287.1; -; Genomic_DNA.
DR RefSeq; XP_448326.1; XM_448326.1.
DR AlphaFoldDB; Q6FN68; -.
DR SMR; Q6FN68; -.
DR STRING; 5478.XP_448326.1; -.
DR EnsemblFungi; CAG61287; CAG61287; CAGL0K02321g.
DR GeneID; 2890303; -.
DR KEGG; cgr:CAGL0K02321g; -.
DR CGD; CAL0134779; CAGL0K02321g.
DR VEuPathDB; FungiDB:CAGL0K02321g; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; Q6FN68; -.
DR OMA; GLQTYFD; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:1990453; C:nucleosome disassembly/reassembly complex; IEA:EnsemblFungi.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0016573; P:histone acetylation; IEA:EnsemblFungi.
DR GO; GO:0016575; P:histone deacetylation; IEA:EnsemblFungi.
DR GO; GO:0060195; P:negative regulation of antisense RNA transcription; IEA:EnsemblFungi.
DR GO; GO:0006337; P:nucleosome disassembly; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0043487; P:regulation of RNA stability; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
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 PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 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..355
FT /note="Chromatin modification-related protein EAF3"
FT /id="PRO_0000088775"
FT DOMAIN 3..77
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 163..353
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 98..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 40740 MW; 9166E03C6A955626 CRC64;
MFEVGGKCLA YHGPLLYEAK ILRRWNPKLE KVEYSVPLKS GEEDGLPESM NREEFYYYIH
YQGWKSSWDE WVSVDRIMEL TEANIELKKQ LVMEAKKASL AQQQKTKNGG SAKRGGGGAH
SESNHGGRRS GSGDRRDSNA EERGIVPSEG PFRTSSVMSY NFSRNKLRIH IPMILESMLV
DDWEIVTKEK KISNLPNPFP VETILDRFYK DVATRTTSPV ELSLVEEYVY GLKQYFNEAI
GNLLLYKLER LQYEQVFYPT PEQQQAMTPV ERSLSGRRPG QLYGVLHLLR LISILPEMLS
NCVGMDTQAI NVILRHTEKL LLWLVDRIED LLPHKVHKSY YTNTSSQYEG VALGL
