ID A0A165JXP7_9BASI Unreviewed; 259 AA.
AC A0A165JXP7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=Chromo domain-containing protein {ECO:0000259|PROSITE:PS50013};
GN ORFNames=CALCODRAFT_489741 {ECO:0000313|EMBL:KZT62404.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT62404.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT62404.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT62404.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV423916; KZT62404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165JXP7; -.
DR STRING; 1353952.A0A165JXP7; -.
DR InParanoid; A0A165JXP7; -.
DR OrthoDB; 5490924at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0000792; C:heterochromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
DR GO; GO:0097159; F:organic cyclic compound binding; 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:SF112; CHROMATOR, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 34..95
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 28861 MW; 0D314A93BF3826B8 CRC64;
MARPRRGQTD VVDDSEVDKT EVESQEEEGD DEGYIVEKLM NVKKIGKSGG FQYLVRWEGY
EAADDTWEPE ENVQSAPAAI TQFWKTHSKL MDKYNVTSDG QPRTDKPSAA TSTQTKAGRA
SAARGAKANG KESSHTTPTV SRTRIRPLTD SPPVSPPHAP ETRTSAAQTA RKRKRDSDDD
DEELQTMTKH MKTEDWESIV ERVSDVTRGR GKARNTLIVT LELSNGSSST STNIECNKRC
PQKMLAFYES KIRFSEVDA
//