ID   A0A0K0ERG8_STRER        Unreviewed;       690 AA.
AC   A0A0K0ERG8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=HATPase_c domain-containing protein {ECO:0000313|WBParaSite:SSTP_0001204800.1};
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_0001204800.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0001204800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   AlphaFoldDB; A0A0K0ERG8; -.
DR   STRING; 6248.A0A0K0ERG8; -.
DR   WBParaSite; SSTP_0001204800.1; SSTP_0001204800.1; SSTP_0001204800.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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; IPR036890; HATPase_C_sf.
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:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 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   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.
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}.
SQ   SEQUENCE   690 AA;  78738 MW;  DAE0974BFE7A6552 CRC64;
     MLSRSLSRVR YYGRVINTID KHTLSISNNR IFNLNQRIAC LSTTATDTKD TSSVEKFEFH
     AEVKNLLNIV AESLYSDQEV FIRELISNAS DAIEKRRCKE MVEPTDASSV GEENPLEIRI
     DADEGNNRIV ITDTGIGMNR EELISCLGTI AKSGSKDFKD INKGKTSAEQ IIGQFGVGFY
     SAFIVADKVK VSTRKWGSKE GFIWIWDGAT GYKIEKVENS IPYGTKIEID LKPGDCSKFS
     KSSTIKDVIS KYSYFVTVPI LLDGERVNTM NALWTKHPRE VTDEMNENFY RQLVKTHHQH
     LAPERPQYTI HYKTDVPLSI RALLYVPTHK VTQLEYAAST SDCTVSLYAR NVLIKANAKE
     LLPRYLRFLV GVVDSEDVPL NLSRELIQMD KVILKLKKVL TEKVMSFFIS QQKKDRVKYI
     DFYNGYSMYF KEGVCLESDH SIKESISNLL LFESSRLKKG DVTTLKEYIG RMKEDQKEIY
     YLYTPNRQLA ESSPYYEMFK NNGYEVLFIY DPADEIVMSH LPQYDRKSLV PVEKWVKDEG
     TKLDSEANKT QSSNLEKEEF LTFVKESLGK MKVDKVQPSY RQSEHPAILT ISNVDHTAVR
     NLIRTGQVKN LDYIGFLQPT LILSMNHPVV VGAMKLRKKN KELAALVMEQ IYDNALISAG
     LMGDSSQMIS RINKVMSGLM EQEKSTILTP
//