ID   A0A3B3WP11_9TELE        Unreviewed;       685 AA.
AC   A0A3B3WP11;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000004555.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000004555.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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; A0A3B3WP11; -.
DR   Ensembl; ENSPMET00000008981.1; ENSPMEP00000004555.1; ENSPMEG00000006322.1.
DR   Proteomes; UP000261480; 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   685 AA;  78241 MW;  8AAD485EFB4D0B72 CRC64;
     RAAGPGGKPR RHPSQRHCRP AVWRSQWSSL GFSQQSFYST QEVEKEPEEE PLHTIITDTE
     SVQGSFSKHE FQAETKKLLD IVARSLYSEK EVFVRELISN GSDALEKLRH KMITAGGETA
     PMEIHLQTDG TKGTFTIQDT GVGMNKEELV ANLGTIARSG SKAFLDALQN QAEASSTIIG
     QFGVGFYSAF MVADRVDVFS RSTEPDAPGY KWSSDGSGLF EIAEASGVQQ GTKIVLHLKD
     DCKEFSSEDR VKEVVTKYSN FVSFPIFLNG RRLNTLQALW MMEPKEISDW QHEEFYRYIA
     QAYDKPRYTL HYRADAPLNI RSIFYVPDAK PSMFDVSREM GSSVALYSRK VLIQTKATDI
     LPKWLRFLRG VVDSEDIPLN LSRELLQESA LIRKLRNVLQ QRVIRFLLDQ SKKDPEKYSK
     FFEDYGLFMR EGIVTTQEQD VKEDIARLLR FESSALPAGQ QTNLMEYGSR MKAGTRNIYY
     LCAPNRHLAE HSPYFEAMKK KDMEVLFCYE QFDELTLLHL REFDKKKLIS VETDIVVDHY
     KEEKFEESKP ASERLTQEQA DDLMAWMKNV LGPRVTNIKL TPRLDTHPAM ITVLEMGAAR
     HFLRTQQLAR TAEERAQILQ PTLELNAGHD LIKKLHSLKD TNSELAGLLL EQIYDNAMIA
     AGLNDDPRPM ISRLNELLAR ALEKH
//