ID   A0A091DPQ8_FUKDA        Unreviewed;       720 AA.
AC   A0A091DPQ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Heat shock protein 75 kDa, mitochondrial {ECO:0000313|EMBL:KFO24791.1};
GN   ORFNames=H920_13787 {ECO:0000313|EMBL:KFO24791.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO24791.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO24791.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO24791.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KN123497; KFO24791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091DPQ8; -.
DR   STRING; 885580.ENSFDAP00000003724; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR003594; HATPase_C.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Stress response {ECO:0000313|EMBL:KFO24791.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          124..277
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   720 AA;  81823 MW;  33E2B639DE125C9F CRC64;
     MARELRAVLL WGRFVRPPLR APVLAAALGG GFWALGAVQE VMLRKPILCS QRSAVQFRSP
     WQQLSSSFYA GRPYSTQAAE DEKEEPLHSI ISSSEAVQGS ISKHEFQAET KKLLDIVACS
     LYSEKEVFIR ELISNASDAL EKLRHKLVSD GQALPEMEIH LQTDTEKGTI TIQDTGIGMT
     QDELVSNLGT IARSGSKAFL EALQDQAEAS SKIIGQFGVG FYSAFMVADR VEVYSRSAAP
     GSPGYQWLSD GSGVFEIAEA SGVRTGTKII IHLKSECKEF ASEARVRDVV TKYSNFVSFP
     LYLNGRRINT LQAIWMMDPK ELNESQHEQF YRYIAQAYDK PRYTLHYKTD APLNIRSIFY
     VPETKPSMFD VSRELGSSVA LYSRKVLIQT KAADILPKWL RFIQGVVDSE DIPLNLSREL
     LQESALIRKL RDVLQQRLIK FFIDQSKKDA EKYAKFFEDY SLFMREGIVT TAEQEVKEDI
     AKLLRYESSA LPAGQLTSLS DYASRMQAGT RNIYYLCAPS RHLAEHSPYY EAMKQKNTEV
     LFCYEQFDEL TLLHLREFDK KKLISVETDI VVDHYKEEKF EDASPDGERL SEKETEELMA
     WMRNVLGSRV TSVKVTLRLD THPAMVTVLE MGAARHFLRM QQLAKTQEER AQLLQPTLEI
     NPRHTLIRKL SELRQREPEL AQLLADQIYE NAMIAAGLID DPRPMVGRLN DLLVKALEKH
//