ID A0A8S1JW48_PARPR Unreviewed; 217 AA.
AC A0A8S1JW48;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=CS domain-containing protein {ECO:0000259|PROSITE:PS51203};
GN ORFNames=PPRIM_AZ9-3.1.T0110281 {ECO:0000313|EMBL:CAD8047144.1};
OS Paramecium primaurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5886 {ECO:0000313|EMBL:CAD8047144.1, ECO:0000313|Proteomes:UP000688137};
RN [1] {ECO:0000313|EMBL:CAD8047144.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAD8047144.1}.
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DR EMBL; CAJJDM010000008; CAD8047144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8S1JW48; -.
DR OMA; QEEPNAG; -.
DR Proteomes; UP000688137; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:TreeGrafter.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:TreeGrafter.
DR GO; GO:0006457; P:protein folding; IEA:TreeGrafter.
DR CDD; cd06465; p23_hB-ind1_like; 1.
DR FunFam; 2.60.40.790:FF:000039; CS domain containing protein; 1.
DR InterPro; IPR007052; CS_dom.
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 PROSITE; PS51203; CS; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000688137}.
FT DOMAIN 4..92
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 115..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..163
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 25531 MW; 49B3390D6CC808D5 CRC64;
MQKTIAPIVK WAQRKDNVFL TVEVRDLKEE KVELTSNSLK FSANAEGVNY VFEINFFSEV
VVEESKWTNY GLNVRFILSK KDKFTSYWTR LIKETHKLQY LQVDWTKYID EDDEAEEGGK
GLDDWDQNKF QNFDHGHDHG HDHGHDHCHD HGHHHGHDHG HGHHHDDEDD EEDQEEPNAG
NIDDLEKEEE VQQNEQAPKE GDQQKQEVEQ EQNQEAK
//