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
//