ID A0A1Y1JMA9_PLAGO Unreviewed; 829 AA.
AC A0A1Y1JMA9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Endoplasmin {ECO:0000313|EMBL:GAW83599.1};
GN ORFNames=PGO_143970 {ECO:0000313|EMBL:GAW83599.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW83599.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) 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}.
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:GAW83599.1}.
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; BDQF01000015; GAW83599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1JMA9; -.
DR EnsemblProtists; GAW83599; GAW83599; PGO_143970.
DR OMA; KWKLMNE; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000195521; 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 Reference proteome {ECO:0000313|Proteomes:UP000195521};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..829
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012237264"
FT DOMAIN 101..257
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 788..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 466..500
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 788..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 95835 MW; E0BD84C44D4249F5 CRC64;
MKLNQVFPYA VLIFIFFINL IQENRNVLCE SNEGGKVEEN DNLKNDELKN DELKNVELKK
DKDSIPEISE SEKPTSGIEQ HQYQTEVTRL MDIIVNSLYT QKEVFLRELI SNAADALEKI
RFMSLSDENV LGDEKKLEIR ISANKEKNIL SITDTGIGMT KEDLINNLGT IAKSGTSNFL
EAISKSGGDM SLIGQFGVGF YSAFLVADKV IVYTKNNNDD QYIWESTADA KFSIYKDPRG
STLKRGTRIS LHLKDDATNL MNDKKLVDLI SKYSQFIQYP IYLLHENVYT EEVLADIAKE
MVNDPNYDSV KVEESDDPNK KTRTVEKKVK KWKLMNEQKP IWLRSPKELS NDDYKKFFSV
LSGYNDEPLY HIHFFAEGEI EFKCLIYIPS RAPSINDQLF TKQNSIKLYV RRVLVADEFV
DFLPRYMSFI KGVVDSDDLP LNVSREQLQQ NKILKAVSKR IVRKILDTFR NLYTEGKKNK
ENLRAELAKE TDEEKKKEIQ KKINEPSTYK LIYKEYRKYL KSGCYEDDIN RSKIVKLLLF
KTMLYPKSIS LDTYVENMKP DQKFIYYASG ESYEYLSKIP QLQIFKKKNI DVVFLTESVD
ESCIQRVQEY EGKKFKSVQK GEITFDLTEE EKKKEEKVKK MYKALIDVIS DTLRNQIFKV
EISRRLVDAP CAVVSTEWGL SGQMEKLMKI NVNNSDQIRA MSGQKILEIN PDHPIMIDLL
KRSVTNPKDT QLTESIKIIY QSAKLASGFD LEDTADLAQI VYDHINQKLG VDNNLKIDDL
DPAIFETKKM ENEDSSDSQK FDEEINIDDE IQKQDTTPAT ESTPKNDEL
//
