ID   A0A2J6SV47_9HELO        Unreviewed;       212 AA.
AC   A0A2J6SV47;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   SubName: Full=HSP20-like chaperone {ECO:0000313|EMBL:PMD54543.1};
GN   ORFNames=K444DRAFT_617894 {ECO:0000313|EMBL:PMD54543.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD54543.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD54543.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD54543.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the p23/wos2 family.
CC       {ECO:0000256|ARBA:ARBA00025733}.
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; KZ613859; PMD54543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6SV47; -.
DR   STRING; 1095630.A0A2J6SV47; -.
DR   InParanoid; A0A2J6SV47; -.
DR   OrthoDB; 782824at2759; -.
DR   Proteomes; UP000235371; Unassembled WGS sequence.
DR   GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR   CDD; cd06465; p23_hB-ind1_like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR045250; p23-like.
DR   PANTHER; PTHR22932:SF1; CO-CHAPERONE PROTEIN DAF-41; 1.
DR   PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000235371}.
FT   DOMAIN          4..103
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          153..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..195
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   212 AA;  23463 MW;  67ABF97606D98464 CRC64;
     MSAPATPEVL WAQRSNKTDA AKNFIYLTIS VPDVQPSHLK LDLKPQSLAF SGHSDSLKRD
     YHLELEFYAE IDKEESKINH TAKNIEIVLR KKELKEEFWP RLLKDAKKVH FLKTDFDKWV
     DEDEQDEAPE DDLGNMGGMG GMPGMGDMSS MMGGAGGDFG GIDFSKLGGG MGGEEGEEEG
     EEDDEDEDMP ELEEDEASSS EKPASSKIEE VA
//