ID Q6TDF9_CRYPV Unreviewed; 552 AA.
AC Q6TDF9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:AAR83923.1};
DE Flags: Fragment;
OS Cryptosporidium parvum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=5807 {ECO:0000313|EMBL:AAR83923.1};
RN [1] {ECO:0000313|EMBL:AAR83923.1}
RP NUCLEOTIDE SEQUENCE.
RA Leander B.S., Keeling P.J.;
RT "Early evolutionary history of dinoflagellates and apicomplexans
RT (Alveolata) as inferred from hsp90 and actin phylogenies.";
RL J. Phycol. 40:341-350(2004).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; AY423866; AAR83923.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6TDF9; -.
DR VEuPathDB; CryptoDB:cgd3_3770; -.
DR VEuPathDB; CryptoDB:CPATCC_0034780; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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.
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 Stress response {ECO:0000313|EMBL:AAR83923.1}.
FT DOMAIN 1..153
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 184..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR83923.1"
FT NON_TER 552
FT /evidence="ECO:0000313|EMBL:AAR83923.1"
SQ SEQUENCE 552 AA; 64048 MW; 32C25BF9F4E79BF6 CRC64;
IFLRELISNA SDALDKIRYE SLTDPEQLKS NEEMHIRIIP DKVNNTLTIE DSGIGMTKNE
LINNLGTIAR SGTKAFMEAI QAGGDVSMIG QFGVGFYSAY LVADKVTVIT KHNGDEQYIW
ESSAGGSFTI TNDTSDNKLQ RGTRIILHLK EDQLDYLEER TLRDLVKKHS EFISFPIELS
VEKTTEKEIT DSDVDEEEEK KEGEDGEDAP KIEEVKEKEP KKKKITEVTQ SWDLLNKNKP
IWMRKPEEVT FEEYSSFYKS ISNDWEDPLA VKHFSVEGQL EFKAILFIPR RAPFDLFETR
KKRNNIKLYV RRVFIVDDCE ELIPEFLGFV RGVVDSEDLP LNISRESLQQ NKILKVIKKN
IVKKCLELIT EITEKPDDYK KFYEQFSKNL KLGIHEDTTN RNKISELLRY QTSKSGEELI
SLREYVDRMK ENQKEIYYIT GESIQAVQNS PFLEKLRKLD YEVIYMVDPI DEYCVQQMKE
FDGKKLRCCT KEGLTLEETA EEKEAFEALQ KEYEPLCQLI KEVLHDKVDK VITSQRISDS
PCVLVTSEFG WS
//
