ID A0A178EGE8_9PLEO Unreviewed; 229 AA.
AC A0A178EGE8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chromo domain-containing protein {ECO:0000259|PROSITE:PS50013};
GN ORFNames=IQ07DRAFT_559028 {ECO:0000313|EMBL:OAL54735.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54735.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL54735.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54735.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441638; OAL54735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EGE8; -.
DR STRING; 765867.A0A178EGE8; -.
DR InParanoid; A0A178EGE8; -.
DR OrthoDB; 5490924at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0000792; C:heterochromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR CDD; cd00024; CD_CSD; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR PANTHER; PTHR22812:SF112; FI06908P; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 51..111
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 25691 MW; FA19C8D12FB1107D CRC64;
MPPLLSEAGD SSGDESLNAQ ELKKAGSAKK APPVDTPAED DGDSEEGEDE YVVEKILGHR
FVKGTLEFDV KWQGYADPKD RTWEPEANMD GAVDVLKEYF ADIGGRPEPK GQKRKGRQSG
VKGDSETPAS TTKRVKQEQP WSPPPGSWEH DVSHVDTVEE TKNPKTGQLE RFAYLVWNNQ
KKTQHPLKHI YQKCPQKMLL YYESHLVFTF TADNNGNEES GADIRMEDD
//