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Database: UniProt
Entry: A0A1J9RTN2_9PEZI
LinkDB: A0A1J9RTN2_9PEZI
Original site: A0A1J9RTN2_9PEZI 
ID   A0A1J9RTN2_9PEZI        Unreviewed;       414 AA.
AC   A0A1J9RTN2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   RecName: Full=Chromatin modification-related protein EAF3 {ECO:0000256|ARBA:ARBA00018505};
GN   ORFNames=BKCO1_4400061 {ECO:0000313|EMBL:OJD31783.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD31783.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD31783.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD31783.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) 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:OJD31783.1}.
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DR   EMBL; MNUE01000044; OJD31783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RTN2; -.
DR   STRING; 236234.A0A1J9RTN2; -.
DR   OrthoDB; 2878816at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd18983; CBD_MSL3_like; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 1.10.274.30; MRG 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   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   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS51640; MRG; 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:UP000183809};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          23..83
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|SMART:SM00298"
FT   REGION          83..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  47113 MW;  3801CCA6A3DB8369 CRC64;
     MAPASQPMFS KDEKALCFHH ELLYEAKVLD VKALDPNDKK SAYLYKVHYK GWKATWDDWV
     PQDRLRKLND ENRELANNLK KELEAMRRGS QAQKTAATSH KKKPEAGSAR GSEGRETPVA
     STSLAGRKRG RDFEVERVLA VEESQSGKRS TQRKGKSQGK QPPEGKSTPK EKGPKKRKRN
     ELGNEAEMMG RPAKGAKLVN QRRTTARLTV LKNWGRSGTG DSDEETFRTR PAIRLHMPDR
     LKSLLVDDWE NITKNLQLIN IPVKVPVSAI LDMYEDQESP KRIPGSAEAD ILEEIIAGVK
     EYFNKALGRI LLYRFERDQY LEIYKRTESP TDALAGKTMC EIYGGEHLLR LFVSLPELIA
     QTNMDPQSVN RLREELVKIT MWLNKDETVG KVFVSEYESP GVEYVDKAKG DEKR
//
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