ID Q5CY50_CRYPI Unreviewed; 787 AA.
AC Q5CY50;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Heat shock protein 90 (Hsp90), signal peptide plus ER retention motif {ECO:0000313|EMBL:EAK90361.1};
GN ORFNames=cgd7_3670 {ECO:0000313|EMBL:EAK90361.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK90361.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK90361.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAK90361.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAEE01000001; EAK90361.1; -; Genomic_DNA.
DR RefSeq; XP_628530.1; XM_628528.1.
DR AlphaFoldDB; Q5CY50; -.
DR SMR; Q5CY50; -.
DR STRING; 353152.Q5CY50; -.
DR EnsemblProtists; EAK90361; EAK90361; cgd7_3670.
DR GeneID; 3372116; -.
DR KEGG; cpv:cgd7_3670; -.
DR VEuPathDB; CryptoDB:cgd7_3670; -.
DR InParanoid; Q5CY50; -.
DR OMA; KWKLMNE; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000006726; Chromosome 7.
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; 2.
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:UP000006726};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:EAK90361.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..787
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004254640"
FT DOMAIN 109..264
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 749..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..787
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 89193 MW; 5D4FDF2C7B31D1B8 CRC64;
MSFLLHLLVF FCLIINLCFG SESTGVPSGA TFDESQLGDL NNIDLSSFGA NGGSFADESE
AVVDSITPAP LPELSNDDEA AIQKTSESYE FQTEVSRLMD IIINSLYSQK DVFLRELLSN
SADALEKARF ISVTDDSFLG EQQELEIRVS FNNDKRTITI SDTGIGMTRH DLVTNLGTVA
KSGTANFLES LAKGGDLNLI GQFGVGFYAS YLVSDRVTVI SKNNEDKQYV WESSADGSFR
VSLDPRGNTI KRGTTIVLSL KEDATEFMNF SKLKDLVLRY SQFINFPIYI YNPEGVNKSE
KDESGEKKES KGRWEQVNVE KAIWLRPREE ITKEEYNGFY KSITHDYSEP LRYLHFSAEG
EIEFKSLLFI PSHPPFDMFD TYMGKSGNIK FYVRRVLITD HIEDLLPKYL NFIKGVVDSD
DISLNVAREH VQQSRIIKVI SKKMVRKVLE MIKQIQTEQL NAEKEEANKP DEEKKKDAAL
TVYDKFYDMF HKNLKLGCYE DDSNRSKIVK LLKFHTSKSG DSTVFLSKYI EGMKPEQKSI
FYISGESPSA LLKNPLVSLY LKHDIEVLFL TEGVDEPCIS RVPELEGFKF TSIEKSDVRP
FEETEEEKNM HKRLSKFYEP LLKFVKDEFP GEFLKVEVSK RLVSDPAVIT SGPWGQSAYM
QKIQKAQTFS NKADYKNKHM EINPNHALIK KLNDLVISKN NVEAKALALK IIQLSTIASG
FDLENPSEFA SGMFKIMLQS SGIDEKDVIS SVELPEEVST DEGVEGSDQE KGFDDEEDEK
NEKRDEL
//
