ID   EAF3_CRYNJ              Reviewed;         305 AA.
AC   P0CO86; B6YPM2; Q55QR4; Q5KFF1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Chromatin modification-related protein EAF3;
GN   Name=EAF3; OrderedLocusNames=CNF01960;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017346; AAW44213.1; -; Genomic_DNA.
DR   EMBL; AE017346; AAW44214.1; -; Genomic_DNA.
DR   RefSeq; XP_571520.1; XM_571520.1.
DR   RefSeq; XP_571521.1; XM_571521.1.
DR   AlphaFoldDB; P0CO86; -.
DR   SMR; P0CO86; -.
DR   STRING; 5207.AAW44213; -.
DR   PaxDb; P0CO86; -.
DR   EnsemblFungi; AAW44213; AAW44213; CNF01960.
DR   GeneID; 3258090; -.
DR   KEGG; cne:CNF01960; -.
DR   VEuPathDB; FungiDB:CNF01960; -.
DR   eggNOG; KOG3001; Eukaryota.
DR   HOGENOM; CLU_039566_1_1_1; -.
DR   InParanoid; P0CO86; -.
DR   OMA; HKFFDIE; -.
DR   OrthoDB; 1624495at2759; -.
DR   Proteomes; UP000002149; Chromosome 6.
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:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
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   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..305
FT                   /note="Chromatin modification-related protein EAF3"
FT                   /id="PRO_0000088776"
FT   DOMAIN          14..67
FT                   /note="Tudor-knot"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          131..304
FT                   /note="MRG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT   REGION          86..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  35135 MW;  0F5ED7BEC60C72D3 CRC64;
     MAGAVPQFMV DEYVLAYHGP LLYEARVILA EVWDESNTLL GTVGPHYFIH YKGWKQTWDE
     WVPESRLLKL NEAGFAKRRA LLDAQAKKGR STGGSGGTGS PGAGKGGLKD KKKDTKKRGR
     DAMESESDFM KRPEVKIVIP DVLKLVLVDD WENVTKNNQL VALPRKPNVR ELLEEYRQYA
     SASKKQERSD RATALLSEII SGITLYFDKA LGNNLLYRFE RAQYVEQKRQ NPEKPMSEIY
     GAEHLLRLFV NFGPFIAYTN IDTESLNILR DYINDIMQWM IKEQKRLFMK EYEETTTHYQ
     NLSRS