ID   A0A0R3RSG6_9BILA        Unreviewed;       675 AA.
AC   A0A0R3RSG6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=HATPase_c domain-containing protein {ECO:0000313|WBParaSite:EEL_0000476801-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000476801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000476801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0R3RSG6; -.
DR   STRING; 1147741.A0A0R3RSG6; -.
DR   WBParaSite; EEL_0000476801-mRNA-1; EEL_0000476801-mRNA-1; EEL_0000476801.
DR   Proteomes; UP000050640; Unplaced.
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}.
SQ   SEQUENCE   675 AA;  76256 MW;  7071156D000D1028 CRC64;
     MASRRGVIVL LRSLHRRPYL MPTSCSFAST AHLFCTTRSA GKPLKAENFE FQAETKNLLD
     IVAKSLYSDQ EVFIRELISN ASDALEKRRC KHLETNQDTN IAYEIKITTD ENAQMIIFED
     NGIGMDKEDL VNCLGTIAKS GSKKFIEEQS SQDRASTESI IGQFGVGFYS AFMVASNVVV
     KTRKEGSDKG YLWKWNGGDV YSVEEIDSLP IGSRIEVTLR SGNAAEFAKK DKVVEVINKY
     SYFITLPITV NGERVNTVDA IWTMNPREVT SEMHDTFFRQ LAKTHSPHLV NDRPQYTIHY
     KADAPINVRS LLYVPSHNVS QLEFASSAEQ SGVSLYARRV LIKSNAKDLL PRYLRFLVGV
     VDSEDIPLNL SREMLQMDAV LVKLRQTLTD KVVSYFVNEM KKDRIKYKEF YNGYSLYFKE
     GVCTENDQNI KEQIGSLLLF ESSGLKAGTF TSLDEYVGRM QKDQNEIYYL FAPSRQLAEH
     SPYYEMFKSE NKEVLFAYDA ADEVCLLAMQ QFRMKSIKSA ENWTRIETGG DSQSTTITIR
     DADKKELLDW LKTTLGSVKV NDIKSSGTAS EHPCMITIGA EMGAARHFLR VGQVKDTEHL
     AFLKPTLHVN LNHPIISALI KLHKSEPTVA GFVAEQIYDN ALITCGLMKD SSKMVDRVNR
     LLTELLKPKS SILTP
//