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Database: UniProt
Entry: C3TTP1_9CRYT
LinkDB: C3TTP1_9CRYT
Original site: C3TTP1_9CRYT 
ID   C3TTP1_9CRYT            Unreviewed;       215 AA.
AC   C3TTP1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=90 kDa heat shock protein {ECO:0000313|EMBL:ACN22064.1};
DE   Flags: Fragment;
GN   Name=hsp90 {ECO:0000313|EMBL:ACN22064.1};
OS   Cryptosporidium suis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=396558 {ECO:0000313|EMBL:ACN22064.1};
RN   [1] {ECO:0000313|EMBL:ACN22064.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=14289 {ECO:0000313|EMBL:ACN22064.1};
RX   PubMed=19168758; DOI=10.1128/EC.00294-08;
RA   Feng Y., Dearen T., Cama V., Xiao L.;
RT   "90-kilodalton heat shock protein, Hsp90, as a target for genotyping
RT   Cryptosporidium spp. known to infect humans.";
RL   Eukaryot. Cell 8:478-482(2009).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; FJ153252; ACN22064.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3TTP1; -.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Stress response {ECO:0000313|EMBL:ACN22064.1}.
FT   DOMAIN          5..160
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          192..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACN22064.1"
FT   NON_TER         215
FT                   /evidence="ECO:0000313|EMBL:ACN22064.1"
SQ   SEQUENCE   215 AA;  24068 MW;  41FFFEC7FE046EFA CRC64;
     SLYSQKDVFL RELLSNSADA LEKARFISVT DDSFLGEQQE LEIRVSFNSD KRTITISDTG
     IGMTRHDLVT NLGTVAKSGT ANFLESLAKG GDLNLIGQFG VGFYASYLVS DRVTVISKNN
     EDKQYVWESS ADGSFRVSLD PRGNTIKRGT TIVLSLKEDA TEFMNFSKLK DLALRYSQFI
     NFPIYIYNPE GVNKSEKDES GEKESKGRWE QVNVE
//
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