ID   HSP90_PLAFP             Reviewed;         193 AA.
AC   P20147;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Heat shock 90 kDa protein homolog;
DE   Flags: Fragment;
OS   Plasmodium falciparum (isolate Palo Alto / Uganda).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=57270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3060854; DOI=10.1093/nar/16.22.10928;
RA   Jendoubi M., Bonnefoy S.;
RT   "Identification of a heat shock-like antigen in P. falciparum, related to
RT   the heat shock protein 90 family.";
RL   Nucleic Acids Res. 16:10928-10928(1988).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle that is linked to its ATPase activity. This cycle
CC       probably induces conformational changes in the client proteins, thereby
CC       causing their activation. Interacts dynamically with various co-
CC       chaperones that modulate its substrate recognition, ATPase cycle and
CC       chaperone function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; X13014; CAA31436.1; -; mRNA.
DR   PIR; S01958; S01958.
DR   AlphaFoldDB; P20147; -.
DR   SMR; P20147; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.120.790; -; 1.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           <1..193
FT                   /note="Heat shock 90 kDa protein homolog"
FT                   /id="PRO_0000062942"
FT   REGION          171..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           189..193
FT                   /note="TPR repeat-binding"
FT   NON_TER         1
SQ   SEQUENCE   193 AA;  21968 MW;  86A5F2DF3A6A9073 CRC64;
     KDFDGKKLKC CTKEGLDIHH SEEAKKDFET LKAEYEGLCK VIKDVLHKKV EKVVVGQRIT
     DSPCVLVTSE FGWSANMERI MKAQALRDNS MTSYMLSKKI MEINARHPII SALKQKADAD
     KSDKTVKYLI WLLFDTSLLT SGFALEEPTT FSKRIHRMIK LGLSIDEEEN NDIDLPPLEE
     TVDATDSKME EVD