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Database: UniProt
Entry: A0A0K0EQK8_STRER
LinkDB: A0A0K0EQK8_STRER
Original site: A0A0K0EQK8_STRER 
ID   A0A0K0EQK8_STRER        Unreviewed;       742 AA.
AC   A0A0K0EQK8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=HATPase_c domain-containing protein {ECO:0000313|WBParaSite:SSTP_0001173800.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0001173800.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0001173800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   AlphaFoldDB; A0A0K0EQK8; -.
DR   STRING; 6248.A0A0K0EQK8; -.
DR   WBParaSite; SSTP_0001173800.1; SSTP_0001173800.1; SSTP_0001173800.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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:SF97; ENDOPLASMIN; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..742
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005328446"
FT   DOMAIN          87..245
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   742 AA;  85969 MW;  01FC60B71A6E6724 CRC64;
     MFGNKIFFLF FILQVFIHFS YSTGTESLSN GTNIQDEEVK KELYEDPPKA YLSKEEIDNM
     TNLGESFQFQ AEISRMMKLI VNSLYKNKEI FMRELVSNAA DALDKIRFLS YRQKDALSAG
     EELVIRIKTD PEANTITITD TGIGMTKNEL ITHLGTIAKS GTAHFIEKII NASNTEEQNN
     LIGQFGVGFY SAFLVSEKVV VRSKHNNDSQ YIWISDSNSY TIIKDPEGDT LKRGTEVTLY
     LKDDAKEYSD RSKVQNLIHS YSQFVTFDIY AYEKQPNDNV KKGDNNNDEV NENATVKYAW
     KKINGFKPLW VRQPKNVTEE EYERFYNGLI INPFERKPYL GRIHFHTEGD VIFKGIFFIP
     GQLNEKMEGN VLSIKKLIKL YVRRIFITDE ISEILPRYLS WVAGVVDSDD LPLNVSREVL
     QTSKLLRLIR KKIVRKILDM ISKLKGEAFD KFYTIYSRKM KHGILEDYEN ANKIAKILRF
     NSSYEGSETS LDDYISRMKD DQKEIYYLGG ESIYEIKTSP LIEKYIQNNI EVLYCLDPLD
     ENVFEQLSIY KNKKFRNLAI SQKDEYNNKS KEVDYDEKEY TVLIDWFKKN IMDDKIEKIV
     LSNRLSSSPA AYVSTEYGIS GYRVKLIRAT QILSKTSADS ILRKLSYNFE INPDNEIIKM
     LLEMIKLDEN DELALKIGHL ISDVAKLRSG FIIDRPDEFG STIDQLIKLN VQSYKKLSTH
     SKNDVDKCDK NKCENKLSHS EL
//
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