ID A0A1E5VXN4_9POAL Unreviewed; 200 AA.
AC A0A1E5VXN4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
DE Flags: Fragment;
GN ORFNames=BAE44_0009115 {ECO:0000313|EMBL:OEL29866.1};
OS Dichanthelium oligosanthes.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL29866.1, ECO:0000313|Proteomes:UP000095767};
RN [1] {ECO:0000313|EMBL:OEL29866.1, ECO:0000313|Proteomes:UP000095767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC TISSUE=Leaf {ECO:0000313|EMBL:OEL29866.1};
RA Studer A.J., Schnable J.C., Brutnell T.P.;
RT "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT species.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a co-chaperone for HSP90.
CC {ECO:0000256|RuleBase:RU369032}.
CC -!- SUBUNIT: Interacts with HSP90 in an ATP-dependent manner.
CC {ECO:0000256|RuleBase:RU369032}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369032}.
CC Nucleus {ECO:0000256|RuleBase:RU369032}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733, ECO:0000256|RuleBase:RU369032}.
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:OEL29866.1}.
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DR EMBL; LWDX02026776; OEL29866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5VXN4; -.
DR STRING; 888268.A0A1E5VXN4; -.
DR OrthoDB; 782824at2759; -.
DR Proteomes; UP000095767; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:UniProtKB-UniRule.
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:SF22; CO-CHAPERONE PROTEIN P23-1; 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 Chaperone {ECO:0000256|RuleBase:RU369032};
KW Cytoplasm {ECO:0000256|RuleBase:RU369032};
KW Nucleus {ECO:0000256|RuleBase:RU369032};
KW Reference proteome {ECO:0000313|Proteomes:UP000095767}.
FT DOMAIN 20..107
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEL29866.1"
SQ SEQUENCE 200 AA; 22062 MW; 4693F802D834DFE6 CRC64;
RDINFLFYVD FLMSGNVFCS RHPEVKWAQR IDKVYITVQL ADAKDAKVNL EPDGVFTFSG
SAGTNLYELK LDLNDKVNVE ASKISVGVRS IFCIVEKAEA KWWKKLVRDD QRAPHFVKVD
WDKWVDEDDD GGDVNLDGMD FSNFGGMGGM GGMGGLGGMG GLGGMGGMGG LGGMGGMGMD
DFEDESDDEG WYFFCSFYRF
//
