EAF3_KLULA
ID EAF3_KLULA Reviewed; 358 AA.
AC Q6CND0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chromatin modification-related protein EAF3;
GN Name=EAF3; OrderedLocusNames=KLLA0E13541g;
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: 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; CR382125; CAG99646.1; -; Genomic_DNA.
DR RefSeq; XP_454559.1; XM_454559.1.
DR AlphaFoldDB; Q6CND0; -.
DR SMR; Q6CND0; -.
DR STRING; 28985.XP_454559.1; -.
DR PRIDE; Q6CND0; -.
DR EnsemblFungi; CAG99646; CAG99646; KLLA0_E13509g.
DR GeneID; 2893794; -.
DR KEGG; kla:KLLA0_E13509g; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; Q6CND0; -.
DR OMA; GLQTYFD; -.
DR Proteomes; UP000000598; Chromosome E.
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; 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..358
FT /note="Chromatin modification-related protein EAF3"
FT /id="PRO_0000088779"
FT DOMAIN 8..84
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 184..356
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 103..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40334 MW; 5D96BC7643AA22D6 CRC64;
MAIVLDGKCL CYHGPLLYEA KVLRVYDEKN QTITSKDYKD VSIDDEKVEF DRPPEHMRQG
QCYFVHYQGW KSSWDEWVGL DRIRPYNDEN LELKKSLVEK ARELKNNGGK KKSGSRPVGR
PSKVEKGKKA ASRTSNSGSG TNTSASSTSA SNPASSSSSG TTAAASSSDK SDRKKATPVL
NKRSHPKIHI KVPISLRSVL VDDWENVTKD RKLVQLPSER PIEHILSQFY ADTSNSTSSV
VEQAQLSEFL QGIKLYFNLS LGKLLLYRLE RIQYAELLKA HSEKQYTEIY GIIHLLRLVT
LLPEMMESSN VDDQTAKILV KQCDILLEWI AINIARKNFP VDPYINTSSQ YEGVALSM