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Database: UniProt
Entry: I1I374_BRADI
LinkDB: I1I374_BRADI
Original site: I1I374_BRADI 
ID   I1I374_BRADI            Unreviewed;       234 AA.
AC   I1I374;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN   Name=100829416 {ECO:0000313|EnsemblPlants:KQJ96251};
GN   ORFNames=BRADI_3g21990v3 {ECO:0000313|EMBL:KQJ96251.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ96251.1};
RN   [1] {ECO:0000313|EMBL:KQJ96251.1, ECO:0000313|EnsemblPlants:KQJ96251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ96251.1,
RC   ECO:0000313|EnsemblPlants:KQJ96251};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ96251.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ96251.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ96251}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ96251};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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}.
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DR   EMBL; CM000882; KQJ96251.1; -; Genomic_DNA.
DR   RefSeq; XP_003573778.1; XM_003573730.3.
DR   AlphaFoldDB; I1I374; -.
DR   STRING; 15368.I1I374; -.
DR   EnsemblPlants; KQJ96251; KQJ96251; BRADI_3g21990v3.
DR   GeneID; 100829416; -.
DR   Gramene; KQJ96251; KQJ96251; BRADI_3g21990v3.
DR   KEGG; bdi:100829416; -.
DR   eggNOG; KOG3158; Eukaryota.
DR   InParanoid; I1I374; -.
DR   OMA; TEYDDMA; -.
DR   OrthoDB; 782824at2759; -.
DR   Proteomes; UP000008810; Chromosome 3.
DR   ExpressionAtlas; I1I374; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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:UP000008810}.
FT   DOMAIN          2..91
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          189..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   234 AA;  24505 MW;  61E0091BE8F70EAA CRC64;
     MSRHPEVKWA QRIDKVYITV QLPDAKDAKV NLEPDGVFSF SATAGSDGNI YESKLDLNDK
     VNVEESKTSV GPRSIFCIVE KAEAKWWNKL VRDDQKAPHF VKVDWDKWVD EDDDGPEVNV
     DGMDFSNMGG MGGMPGMGGM PGMEGLGGMP GMEALGGMGG LAGMGGMGGM GGMGGMGGMG
     GMGGMGGMGG MGMPPGMGMD DFDDESDDEE EVSKPQDAGK ADAAEKSQEE AKAT
//
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