GenomeNet

Database: UniProt
Entry: A0A178EGE8_9PLEO
LinkDB: A0A178EGE8_9PLEO
Original site: A0A178EGE8_9PLEO 
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
//
DBGET integrated database retrieval system