ID   B6AIL0_CRYMR            Unreviewed;       705 AA.
AC   B6AIL0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Hsp90 protein, putative {ECO:0000313|EMBL:EEA08051.1};
GN   ORFNames=CMU_031920 {ECO:0000313|EMBL:EEA08051.1};
OS   Cryptosporidium muris (strain RN66).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN   [1] {ECO:0000313|EMBL:EEA08051.1, ECO:0000313|Proteomes:UP000001460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN66 {ECO:0000313|EMBL:EEA08051.1,
RC   ECO:0000313|Proteomes:UP000001460};
RA   Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA   da Silva J.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; DS989736; EEA08051.1; -; Genomic_DNA.
DR   RefSeq; XP_002142400.1; XM_002142364.1.
DR   AlphaFoldDB; B6AIL0; -.
DR   STRING; 441375.B6AIL0; -.
DR   EnsemblProtists; EEA08051; EEA08051; CMU_031920.
DR   GeneID; 6997486; -.
DR   VEuPathDB; CryptoDB:CMU_031920; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 547579at2759; -.
DR   Proteomes; UP000001460; Unassembled WGS sequence.
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; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; 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   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001460}.
FT   DOMAIN          25..180
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          211..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  81101 MW;  C0BE3ECB97148393 CRC64;
     MVETFAFNAD IQQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT DPDQLKTNED
     LYIRIIPDKV NNTLTIEDSG IGMTKNELIN NLGTIARSGT KAFMEAIQAG GDISMIGQFG
     VGFYSAYLVA DKVTVITKHN GEGQYIWESS AGGSFTITED SSDNSLSRGT RIVLHLKEDQ
     LEYLEERALR DLVKKHSEFI SFPIQLSVEK TTEKEVTDSD VDEEEDKEDK GDSEETKEGE
     DAPKIEEVKE EKPKKKTITE VTKSWDLLNK NKPIWMRKPE EVVFEEYSSF YKSISNDWED
     PLAIKHFSVE GQLEFKSILF IPRRAPFDLF ETRKKRNNIK LYVRRVFIMD DCEELIPEYL
     GFVRGVVDSE DLPLNISRES LQQNKILKVI KKNIVKKCLE LISEITEKPE DYKKFYEQFS
     KNLKLGIHED SANRNKISEL LRYQTSKSGD EMISLKEYVD RMKEGQKEIY YITGESIQVV
     QNSPFLERLR KLGYEVLYMV DPIDEYCVQQ LKEFEGKKLR CCTKEGLTLE ETAEEKEAFE
     NIQKEFEPLC QLIKEVLHDK VDKVVVSQRI SDSPCVLVTS EYGWSANMER IMKAQALRDT
     SMTSYMMSRK TMEINPHNSI MAELNSKIAA DKSDKTVKDL IWLLYDTSLL TSGFSLDEPT
     QFASRINRMI KLGLSIDEDD VADDLPALEE VNDATVQASK MEEVD
//