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Database: UniProt
Entry: A0A1Y2VZW5_9PEZI
LinkDB: A0A1Y2VZW5_9PEZI
Original site: A0A1Y2VZW5_9PEZI 
ID   A0A1Y2VZW5_9PEZI        Unreviewed;       249 AA.
AC   A0A1Y2VZW5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Chromo domain-containing protein {ECO:0000259|PROSITE:PS50013};
GN   ORFNames=M426DRAFT_322906 {ECO:0000313|EMBL:OTB02197.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB02197.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB02197.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB02197.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KZ111572; OTB02197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VZW5; -.
DR   STRING; 1001833.A0A1Y2VZW5; -.
DR   InParanoid; A0A1Y2VZW5; -.
DR   OrthoDB; 5490924at2759; -.
DR   Proteomes; UP000242955; 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   CDD; cd18657; CSD_Swi6; 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:UP000242955}.
FT   DOMAIN          67..129
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..64
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  27722 MW;  FA896896DD0CB7EF CRC64;
     MPPAISEDEA SEVGEISVPL RSTREKKSSA NLDNDDDFTN VAEDDAQNGD DDQDEEGGAE
     DMEEDEFIVE KILAHVVEPD GALRYRVKWE GYEKKADQTW EDEENLKENA SDVLEEYLKN
     VGGREKIIED SKAALKTKKR GRPSSSATPT NGTKRRRGGS HPDSATPPTT GRTWAPPAGS
     WEDAVDAIDA CHDENTGKLI VYLTWKDGHK TQHDTKAVYK RCPQKMLQFY ERHVKIVMSG
     SDGGLKEEA
//
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