EAF3_DICDI
ID EAF3_DICDI Reviewed; 379 AA.
AC Q54RM0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=NuA4 complex subunit EAF3 homolog;
GN ORFNames=DDB_G0283075;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. Also a component of a complex which acts
CC to repress transcription by deacetylation of nucleosomal histones (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}.
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DR EMBL; AAFI02000049; EAL65981.1; -; Genomic_DNA.
DR RefSeq; XP_639331.1; XM_634239.1.
DR AlphaFoldDB; Q54RM0; -.
DR SMR; Q54RM0; -.
DR STRING; 44689.DDB0267076; -.
DR PaxDb; Q54RM0; -.
DR EnsemblProtists; EAL65981; EAL65981; DDB_G0283075.
DR GeneID; 8623902; -.
DR KEGG; ddi:DDB_G0283075; -.
DR dictyBase; DDB_G0283075; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_1_1; -.
DR InParanoid; Q54RM0; -.
DR OMA; GLQTYFD; -.
DR PhylomeDB; Q54RM0; -.
DR PRO; PR:Q54RM0; -.
DR Proteomes; UP000002195; Chromosome 4.
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: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:0040008; P:regulation of growth; 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; Growth regulation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..379
FT /note="NuA4 complex subunit EAF3 homolog"
FT /id="PRO_0000330868"
FT DOMAIN 6..61
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 214..377
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 75..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 43484 MW; F69AA1D120CDFD95 CRC64;
MDETYEENEK VLVHHQNRIY EAKIIKVDPK TSKSDKKKPL YFIHYLGWKE KWNEWIEPNK
ILKYTDKNRE LQKRTNIKAS TTSLNNKKNT KKAKEVKQQQ QQQQPIAYDS ENSDEDENES
ELEDGGGEDA DEGGEDIEDQ ENNNNNDTGG EEADDNNTSP RSTGSSSSSS SSKSNNNNNN
NNNNNNNNNN NNNNNNNNNN KRKRNDSKSS HFQSTKFIDI EIPLSLKNKL VDDWNSINNE
KSILSLPKSP NVKDILNKII EENDKSSECK EVINGIKQYF NKALGTLLLY KFERPQYDSI
LKTNPKKSMS DIYGAEHLLR LFVKLPQLLV ISNLEEKTIT QLKDAFEIVL EYLEKNSSTL
FLKEYTIASS PYLKAASSN
