ID A0A0G2FDX6_9PEZI Unreviewed; 967 AA.
AC A0A0G2FDX6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=Chromatin modification-related protein EAF3 {ECO:0000256|ARBA:ARBA00018505};
GN ORFNames=UCDDA912_g07234 {ECO:0000313|EMBL:KKY32792.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY32792.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY32792.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32792.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY32792.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY32792.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000256|ARBA:ARBA00011353}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MRG family. {ECO:0000256|ARBA:ARBA00009093}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY32792.1}.
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DR EMBL; LCUC01000279; KKY32792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FDX6; -.
DR STRING; 1214573.A0A0G2FDX6; -.
DR OrthoDB; 2878816at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd18983; CBD_MSL3_like; 1.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.274.30; MRG domain; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 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 InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR10880; MORTALITY FACTOR 4-LIKE PROTEIN; 1.
DR PANTHER; PTHR10880:SF15; MRG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS51640; MRG; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 528..557
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 79..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 107676 MW; B33BF39F9848BCE8 CRC64;
MAPSSKPSAP PYAKDEKVLC FHHDMLYEAK IIEIDSTEEG GFRYKIHYKG WKATWDDWVP
QDRIRKLNDE NRELAAQLNQ QARASMQKKS GPAKKAGLKN GSDFSSARGS EERSGAAATM
SGRGRKRDFD LENPNTTTNE AVFTKGAQLS NLKVNIFKCA TFYSVPLILI PSLIVHVDLM
DSAFVKKEAN WYKASLRYDN LSNLPPEILS KSNPGLKEAL RDFYFTSTDE GLKVKQKAED
RFDPWPAPYR RAKPKKREET PEDNEELLTA GIPPKDREAF NEELRSFMQE NCPSEVEELP
DPIVTKTVKA EKAKKAVINR ENRAAAKARS TMPPAQHTRN TRLRTKAAQA IAAADGQAPA
GNATATQNAT AAVVTPGAEE NTARSRQHSA PPFNLFMRDT RASMDRNAFM SRPVQGVVPN
SYYAAFNNAY NSVYPKARSV GDEPIGNDIP SSPAKGREPA GSKEAPTTTA PKKSAAPKAA
AAASKTAAPK KSAATKTTTS KTASTKPVQG SLDKDMSAAM KLPRAAKACD PCRQHKTRCT
GGTPCEACVR RGFTCVYVPG GRKAPMKRAR EDSQDVVKKE PLENGAEQEG RPAKRARKEQ
AISTKNNSAE GSVGMVGAMD AQTSNILPSI EEVPEDNEGP NAQPSKMHHF SKPKIGKSVT
MQPAKIHFSY SGRVTRSRSR QLSEEAEAQT AKLQYKGKRA REETEEPQER PAKLQRATRK
GPNYRKPDGN PQILRVIDSM AVDSQGNAQT DSPWDNYDYE PTWMSHTYLK WKDSVVCPGF
NLKSQDESFH ARPSIKLVMT DVLKGILVDD WEHVTKDSQL VPLPHEQPVV KILNDYLDDE
MPKRDEDSAQ IDILKETMAG LREYFDRALG RILLYRFERL QYSELLPQWE NEKDGGPSNV
YGGEHLCRLL VSLPELLAQT NMDQQSVSRL REELTKFTNW LSKNGQKYFV REYEVPGPEY
QDKAKSS
//
