ID W7AJR7_9APIC Unreviewed; 814 AA.
AC W7AJR7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Heat shock protein 90kDa beta {ECO:0000313|EMBL:EUD69074.1};
GN ORFNames=C922_00766 {ECO:0000313|EMBL:EUD69074.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD69074.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD69074.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD69074.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-2013) 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; KI965461; EUD69074.1; -; Genomic_DNA.
DR RefSeq; XP_008814600.1; XM_008816378.1.
DR AlphaFoldDB; W7AJR7; -.
DR EnsemblProtists; EUD69074; EUD69074; C922_00766.
DR GeneID; 20036040; -.
DR VEuPathDB; PlasmoDB:C922_00766; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000030640; 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; 3.30.70.2140; -; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:EUD69074.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..814
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004888003"
FT DOMAIN 88..244
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 34..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..487
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 93739 MW; FEA940BF9B039666 CRC64;
MKLNRVFPCA LLIGALLPSW VPRNFNVLCE SNEGKVEDNG SKEEIKKDTD SIPEISDNEK
PTSGIEQHQY QTEVTRLMDI IVNSLYTQKE VFLRELISNA ADALEKIRFM SLSDEKVLGE
EKKLEIRISA NKEKNILSIT DTGIGMTKED LINNLGTIAK SGTSNFLEAI SKSGGDMSLI
GQFGVGFYSA FLVADKVIVY TKNNNDEQYI WESTADAKFS IYKDPRGSTL KRGTKISLHL
KDDATNLMND KKLVDLISKY SQFIQYPIYL LHENVYTEEV LADIAKEMEN DPNYDSVKVE
ETDDPNKKTR TVEKKVKKWK LMNEQKPIWL RPPKELTDAD YKKFFSVLSG YNDEPLYHIH
FFAEGEIEFK CLIYIPSRAP SINDHLFTKQ NSIKLYVRRV LVADEFVEFL PRYMSFVKGV
VDSDDLPLNV SREQLQQNKI LKAVSKRIVR KILDTFRTLY TNGKKNKEDL RAQLAKETDE
EKKKEIEKKI NEPSTYKLIY KEYRKYLKTG CYEDDINRSK IVKLLLFKTM LHPKSISLDT
YVENMKPDQK FIYYASGESY EYLSKIPQLQ IFKKKNIDVV FLTESVDESC VQRVQEYDGK
KFKSIQKGEI TFDLTDDEKK KEEKVKKMYK ALIDVISDTL RNQIFKVEIS RRLVDAPCAV
VSTEWGLSGQ MEKLMKINVN NAEQIRAMSG QKILEINPDH PIMIDLLKRS VSNPKDSQLT
ESIKIIYQSA KLASGFDLED TADLAQIVYD HINQKLGVDN NLKIDDLDPA IFETKKMEQE
DSAEGQTFHE EINIEDEIQK QDSATESAPK NDEL
//
